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

<p>Describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.</p><p><a href='../manual/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationⁱ

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.</p><p><a href='../manual/ca_bind' target='_top'>More...</a></p>Calcium bindingi	646 – 657	12	Sequence Analysis			Add BLAST

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. alpha-actinin binding Source: BHF-UCL

   <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ

   • 17944866

2. calcium activated cation channel activity Source: BHF-UCL

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 10517637
   • 11959145

3. calcium-activated potassium channel activity Source: BHF-UCL

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 10517637

4. calcium channel activity Source: UniProtKB

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 24336289

5. calcium ion binding Source: UniProtKB

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 22193359

6. cation channel activity Source: BHF-UCL

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 17944866

7. cytoskeletal protein binding Source: UniProtKB

   <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ

   • 12809519

8. identical protein binding Source: BHF-UCL
9. muscle alpha-actinin binding Source: BHF-UCL

   <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ

   • 17944866

10. sodium channel activity Source: BHF-UCL

    <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

    • 10517637

11. sour taste receptor activity Source: Ensembl

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. cation transport Source: BHF-UCL
2. cellular response to acidic pH Source: BHF-UCL
3. detection of chemical stimulus involved in sensory perception of sour taste Source: BHF-UCL
4. detection of mechanical stimulus Source: RefGenome
5. potassium ion transmembrane transport Source: BHF-UCL

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 10517637

6. protein homotrimerization Source: UniProtKB

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 22193359

7. sensory perception of sour taste Source: UniProtKB

   <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

   • 19812697

8. smoothened signaling pathway Source: UniProtKB
9. sodium ion transmembrane transport Source: BHF-UCL

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 10517637

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - Molecular functionⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - Biological processⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - Ligandⁱ

Protein family/group databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

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

Topology

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	1 – 103	103	CytoplasmicSequence Analysis			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	104 – 124	21	HelicalSequence Analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	125 – 313	189	ExtracellularSequence Analysis			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	314 – 334	21	HelicalSequence Analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	335 – 347	13	CytoplasmicSequence Analysis			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	348 – 368	21	HelicalSequence Analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	369 – 384	16	ExtracellularSequence Analysis			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	385 – 405	21	HelicalSequence Analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	406 – 476	71	CytoplasmicSequence Analysis			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	477 – 497	21	HelicalSequence Analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	498 – 539	42	ExtracellularSequence Analysis			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	540 – 560	21	HelicalSequence Analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	561 – 805	245	CytoplasmicSequence Analysis			Add BLAST

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. calcium channel complex Source: UniProtKB

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 24336289

2. cell surface Source: Ensembl
3. ciliary membrane Source: UniProtKB-SubCell
4. endoplasmic reticulum Source: BHF-UCL
5. integral component of membrane Source: UniProtKB

   <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ

   • 9878261

6. intracellular membrane-bounded organelle Source: BHF-UCL

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 17944866

7. membrane Source: UniProtKB

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 19812697

8. nonmotile primary cilium Source: UniProtKB

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 24336289

9. plasma membrane Source: UniProtKB

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 20538909

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Provides information on the disease(s) and phenotype(s) associated with the deficiency of a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	523 – 525	3	DFD → AFA: Abolishes ion channel activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.18 "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] Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PKD1L1, SUBCELLULAR LOCATION, MUTAGENESIS OF 523-GLU--GLU-525.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	523 – 523	1	D → Q: Increased permeability of dimethylamine and trimethylamine and decreased permeability of magnesium. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.20 "Molecular mechanism of the assembly of an acid-sensing receptor ion channel complex." Yu Y., Ulbrich M.H., Li M.H., Dobbins S., Zhang W.K., Tong L., Isacoff E.Y., Yang J. Nat. Commun. 3:1252-1252(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 699-743, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-523 AND ASP-525.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	525 – 525	1	D → K: Increased permeability of dimethylamine and trimethylamine and decreased permeability of magnesium. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.20 "Molecular mechanism of the assembly of an acid-sensing receptor ion channel complex." Yu Y., Ulbrich M.H., Li M.H., Dobbins S., Zhang W.K., Tong L., Isacoff E.Y., Yang J. Nat. Commun. 3:1252-1252(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 699-743, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-523 AND ASP-525.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	530 – 530	1	D → A: Does not affect ion channel activity.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	710 – 710	1	L → A: Abolishes homotrimer formation; when assocaited with A-714; A-717; A-728; A-731 and A-735. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.19 "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] Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 699-737, SUBUNIT, CALCIUM-BINDING, MUTAGENESIS OF LEU-710; VAL-714; LEU-717; ILE-728; VAL-731 AND LEU-735.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	714 – 714	1	V → A: Abolishes homotrimer formation; when assocaited with A-710; A-717; A-728; A-731 and A-735. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.19 "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] Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 699-737, SUBUNIT, CALCIUM-BINDING, MUTAGENESIS OF LEU-710; VAL-714; LEU-717; ILE-728; VAL-731 AND LEU-735.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	717 – 717	1	L → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-728; A-731 and A-735. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.19 "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] Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 699-737, SUBUNIT, CALCIUM-BINDING, MUTAGENESIS OF LEU-710; VAL-714; LEU-717; ILE-728; VAL-731 AND LEU-735.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	728 – 728	1	I → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-731 and A-735. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.19 "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] Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 699-737, SUBUNIT, CALCIUM-BINDING, MUTAGENESIS OF LEU-710; VAL-714; LEU-717; ILE-728; VAL-731 AND LEU-735.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	731 – 731	1	V → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-728 and A-735. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.19 "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] Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 699-737, SUBUNIT, CALCIUM-BINDING, MUTAGENESIS OF LEU-710; VAL-714; LEU-717; ILE-728; VAL-731 AND LEU-735.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	735 – 735	1	L → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-728 and A-731. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.19 "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] Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 699-737, SUBUNIT, CALCIUM-BINDING, MUTAGENESIS OF LEU-710; VAL-714; LEU-717; ILE-728; VAL-731 AND LEU-735.

Organism-specific databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	1 – 805	805	Polycystic kidney disease 2-like 1 protein		PRO_0000164360	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	177 – 177	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	207 – 207	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	241 – 241	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	505 – 505	1	N-linked (GlcNAc...)Sequence Analysis

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - PTMⁱ

Proteomic databases

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

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.</p><p><a href='../manual/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

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

<p>Provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	704 – 731	28	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:3TE3
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	734 – 741	8	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:4GIF

3D structure databases

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

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	633 – 668	36	EF-hand			Add BLAST

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	704 – 763	60	Required for protein homotrimerization			Add BLAST

Coiled coil

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Denotes the positions of regions of coiled coil within the protein.</p><p><a href='../manual/coiled' target='_top'>More...</a></p>Coiled coili	650 – 686	37	Sequence Analysis			Add BLAST

Motif

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.</p><p><a href='../manual/motif' target='_top'>More...</a></p>Motifi	195 – 207	13	Polycystin motif			Add BLAST

<p>Provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.</p><p><a href='../manual/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>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 length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (5)ⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry describes 5<p>Lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.</p><p><a href='../manual/alternative_products' target='_top'>More...</a></p> isoformsⁱ produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

        10         20         30         40         50
MNAVGSPEGQ ELQKLGSGAW DNPAYSGPPS PHGTLRVCTI SSTGPLQPQP 
        60         70         80         90        100
KKPEDEPQET AYRTQVSSCC LHICQGIRGL WGTTLTENTA ENRELYIKTT 
       110        120        130        140        150
LRELLVYIVF LVDICLLTYG MTSSSAYYYT KVMSELFLHT PSDTGVSFQA 
       160        170        180        190        200
ISSMADFWDF AQGPLLDSLY WTKWYNNQSL GHGSHSFIYY ENMLLGVPRL 
       210        220        230        240        250
RQLKVRNDSC VVHEDFREDI LSCYDVYSPD KEEQLPFGPF NGTAWTYHSQ 
       260        270        280        290        300
DELGGFSHWG RLTSYSGGGY YLDLPGSRQG SAEALRALQE GLWLDRGTRV 
       310        320        330        340        350
VFIDFSVYNA NINLFCVLRL VVEFPATGGA IPSWQIRTVK LIRYVSNWDF 
       360        370        380        390        400
FIVGCEVIFC VFIFYYVVEE ILELHIHRLR YLSSIWNILD LVVILLSIVA 
       410        420        430        440        450
VGFHIFRTLE VNRLMGKLLQ QPNTYADFEF LAFWQTQYNN MNAVNLFFAW 
       460        470        480        490        500
IKIFKYISFN KTMTQLSSTL ARCAKDILGF AVMFFIVFFA YAQLGYLLFG 
       510        520        530        540        550
TQVENFSTFI KCIFTQFRII LGDFDYNAID NANRILGPAY FVTYVFFVFF 
       560        570        580        590        600
VLLNMFLAII NDTYSEVKEE LAGQKDELQL SDLLKQGYNK TLLRLRLRKE 
       610        620        630        640        650
RVSDVQKVLQ GGEQEIQFED FTNTLRELGH AEHEITELTA TFTKFDRDGN 
       660        670        680        690        700
RILDEKEQEK MRQDLEEERV ALNTEIEKLG RSIVSSPQGK SGPEAARAGG 
       710        720        730        740        750
WVSGEEFYML TRRVLQLETV LEGVVSQIDA VGSKLKMLER KGWLAPSPGV 
       760        770        780        790        800
KEQAIWKHPQ PAPAVTPDPW GVQGGQESEV PYKREEEALE ERRLSRGEIP 

TLQRS                                             

        10         20         30         40         50
MNAVGSPEGQ ELQKLGSGAW DNPAYSGPPS PHGTLRVCTI SSTGPLQPQP 
        60         70         80         90        100
KKPEDEPQET AYRTQVSSCC LHICQGIRGL WGTTLTENTA ENRELYIKTT 
       110        120        130        140        150
LRELLVYIVF LVDICLLTYG MTSSSAYYYT KVMSELFLHT PSDTGVSFQA 
       160        170        180        190        200
ISSMADFWDF AQGPLLDSLY WTKWYNNQSL GHGSHSFIYY ENMLLGVPRL 
       210        220        230        240        250
RQLKVRNDSC VVHEDFREDI LSCYDVYSPD KEEQLPFGPF NGTAWTYHSQ 
       260        270        280        290        300
DELGGFSHWG RLTSYSGGGY YLDLPGSRQG SAEALRALQE GLWLDRGTRV 
       310        320        330        340        350
VFIDFSVYNA NINLFCVLRL VVEFPATGGA IPSWQIRTVK LIRYVSNWDF 
       360        370        380        390        400
FIVGCEVIFC VFIFYYVVEE ILELHIHRLR YLSSIWNILD LVVILLSIVA 
       410        420        430        440        450
VGFHIFRTLE VNRLMGKLLQ QPNTYADFEF LAFWQTQYNN MNAVNLFFAW 
       460        470        480        490        500
IKIFKYISFN KTMTQLSSTL ARCAKDILGF AVMFFIVFFA YAQLGYLLFG 
       510        520        530        540        550
TQVENFSTFI KCIFTQFRII LGDFDYNAID NANRILGPAY FVTYVFFVFF 
       560        570        580        590        600
VLLNMFLAII NDTYSEVKEE LAGQKDELQL SDLLKQGYNK TLLRLRLRKE 
       610        620        630        640        650
RVSDVQKVLQ GGEQEIQFED FTNTLRELGH AEHEITELTA TFTKFDRDGN 
       660        670        680        690        700
RILDEKEQEK MRQDLEEERV ALNTEIEKLG RSIVSSPQGK SGPEAARAGG 
       710        720        730        740        750
WVSGEEFYML TRRVLQLETV LEGVVSQIDA VGSKLKMLER KGWLAPSPGV 
       760
RFPIKEKRKP                                             

        10         20         30         40         50
MNAVGSPEGQ ELQKLGSGAW DNPAYSGPPS PHGTLRVCTI SSTGPLQPQP 
        60         70         80         90        100
KKPEDEPQET AYRTQVSSCC LHICQGIRGL WGTTLTENTA ENRELYIKTT 
       110        120        130        140        150
LRELLVYIVF LVDICLLTYG MTSSSAYYYT KVMSELFLHT PSDTGVSFQA 
       160        170        180        190        200
ISSMADFWDF AQGPLLDSLY WTKWYNNQSL GHGSHSFIYY ENMLLGVPRL 
       210        220        230        240        250
RQLKVRNDSC VVHEDFREDI LSCYDVYSPD KEEQLPFGPF NGTALVVEFP 
       260        270        280        290        300
ATGGAIPSWQ IRTVKLIRYV SNWDFFIVGC EVIFCVFIFY YVVEEILELH 
       310        320        330        340        350
IHRLRYLSSI WNILDLVVIL LSIVAVGFHI FRTLEVNRLM GKLLQQPNTY 
       360        370        380        390        400
ADFEFLAFWQ TQYNNMNAVN LFFAWIKIFK YISFNKTMTQ LSSTLARCAK 
       410        420        430        440        450
DILGFAVMFF IVFFAYAQLG YLLFGTQVEN FSTFIKCIFT QFRIILGDFD 
       460        470        480        490        500
YNAIDNANRI LGPAYFVTYV FFVFFVLLNM FLAIINDTYS EVKEELAGQK 
       510        520        530        540        550
DELQLSDLLK QGYNKTLLRL RLRKERVSDV QKVLQGGEQE IQFEDFTNTL 
       560        570        580        590        600
RELGHAEHEI TELTATFTKF DRDGNRILDE KEQEKMRQDL EEERVALNTE 
       610        620        630        640        650
IEKLGRSIVS SPQGKSGPEA ARAGGWVSGE EFYMLTRRVL QLETVLEGVV 
       660        670        680        690        700
SQIDAVGSKL KMLERKGWLA PSPGVKEQAI WKHPQPAPAV TPDPWGVQGG 
       710        720        730
QESEVPYKRE EEALEERRLS RGEIPTLQRS                       

        10         20         30         40         50
MNAVGSPEGQ ELQKLGSGAW DNPAYSGPPS PHGTLRVCTI SSTGPLQPQP 
        60         70         80         90        100
KKPEDEPQET AYRTQVSSCC LHICQGIRGL WGTTLTENTA ENRELYIKTT 
       110        120        130        140        150
LRELLVYIVF LVDICLLTYG MTSSSAYYYT KVMSELFLHT PSDTGVSFQA 
       160        170        180        190        200
ISSMADFWDF AQGPLLDSLY WTKWYNNQSL GHGSHSFIYY ENMLLGVPRL 
       210        220        230        240        250
RQLKVRNDSC VVHEDFREDI LSCYVSNWDF FIVGCEVIFC VFIFYYVVEE 
       260        270        280        290        300
ILELHIHRLR YLSSIWNILD LVVILLSIVA VGFHIFRTLE VNRLMGKLLQ 
       310        320        330        340        350
QPNTYADFEF LAFWQTQYNN MNAVNLFFAW IKIFKYISFN KTMTQLSSTL 
       360        370        380        390        400
ARCAKDILGF AVMFFIVFFA YAQLGYLLFG TQVENFSTFI KCIFTQFRII 
       410        420        430        440        450
LGDFDYNAID NANRILGPAY FVTYVFFVFF VLLNMFLAII NDTYSEVKEE 
       460        470        480        490        500
LAGQKDELQL SDLLKQGYNK TLLRLRLRKE RVSDVQKVLQ GGEQEIQFED 
       510        520        530        540        550
FTNTLRELGH AEHEITELTA TFTKFDRDGN RILDEKEQEK MRQDLEEERV 
       560        570        580        590        600
ALNTEIEKLG RSIVSSPQGK SGPEAARAGG WVSGEEFYML TRRVLQLETV 
       610        620        630        640        650
LEGVVSQIDA VGSKLKMLER KGWLAPSPGV KEQAIWKHPQ PAPAVTPDPW 
       660        670        680 
GVQGGQESEV PYKREEEALE ERRLSRGEIP TLQRS            

        10         20         30         40         50
MNAVGSPEGQ ELQKLGSGAW DNPAYSGPPS PHGTLRVCTI SSTGPLQPQP 
        60         70         80         90        100
KKPEDEPQET AYRTQVSSCC LHICQGIRGL WGTTLTENTA ENRELYIKTT 
       110        120        130        140        150
LRELLVYIVF LVDICLLTYG MTSSSAYYYT KVMSELFLHT PSDTGVSFQA 
       160        170        180        190        200
ISSMADFWDF AQGPLLDSLY WTKWYNNQSL GHGSHSFIYY ENMLLGVPRL 
       210        220        230        240        250
RQLKVRNDSC VVHEDFREDI LSCYDVYSPD KEEQLPFGPF NGTAWTYHSQ 
       260        270        280        290        300
DELGGFSHWG RLTSYSGGGY YLDLPGSRQG SAEALRALQE GLWLDRGTRV 
       310        320        330        340        350
VFIDFSVYNA NINLFCVLRL VVEFPATGGA IPSWQIRTVK LIRYVSNWDF 
       360        370        380        390        400
FIVGCEVIFC VFIFYYVVEE ILELHIHRLR YLSSIWNILD LVVILLSIVA 
       410        420        430        440        450
VGFHIFRTLE VNRLMGKLLQ QPNTYADFEF LAFWQTQYNN MNAVNLFFAW 
       460        470        480        490        500
IKIFKYISFN KTMTQLSSTL ARCAKDILGF AVMFFIVFFA YAQLGYLLFG 
       510        520        530        540        550
TQVENFSTFI KCIFTQFRII LGDFDYNAID NANRILGPAY FVTYVFFVFF 
       560        570        580        590        600
VLLNMFLAII NDTYSEVKEE LAGQKDELQL SDLLKQGYNK TLLRLRLRKE 
       610        620        630        640        650
RVSDVQKVLQ GGEQEIQFED FTNTLRELGH AEHEITEEER VALNTEIEKL 
       660        670        680        690        700
GRSIVSSPQG KSGPEAARAG GWVSGEEFYM LTRRVLQLET VLEGVVSQID 
       710        720        730        740        750
AVGSKLKMLE RKGWLAPSPG VKEQAIWKHP QPAPAVTPDP WGVQGGQESE 
       760        770 
VPYKREEEAL EERRLSRGEI PTLQRS                       

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	13 – 13	1	Q → H in AAD41638. (PubMed:9748274)Curated

Natural variant

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	278 – 278	1	R → Q. Corresponds to variant rs17112895 [ dbSNP | Ensembl ].		VAR_050555
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	378 – 378	1	R → W. Corresponds to variant rs7909153 [ dbSNP | Ensembl ].		VAR_050556
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	393 – 393	1	V → I.1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.1 "Identification of PKDL, a novel polycystic kidney disease 2-like gene whose murine homologue is deleted in mice with kidney and retinal defects." Nomura H., Turco A.E., Pei Y., Kalaydjieva L., Schiavello T., Weremowicz S., Ji W., Morton C.C., Meisler M., Reeders S.T., Zhou J. J. Biol. Chem. 273:25967-25973(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT ILE-393. Corresponds to variant rs2278842 [ dbSNP | Ensembl ].		VAR_024569
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	681 – 681	1	R → L. Corresponds to variant rs6584356 [ dbSNP | Ensembl ].		VAR_024570
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	788 – 788	1	A → D. Corresponds to variant rs12782963 [ dbSNP | Ensembl ].		VAR_050557

Alternative sequence

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	225 – 344	120	Missing in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.7 "Genes homologous to the autosomal dominant polycystic kidney disease genes (PKD1 and PKD2)." Veldhuisen B., Spruit L., Dauwerse H.G., Breuning M.H., Peters D.J.M. Eur. J. Hum. Genet. 7:860-872(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-805 (ISOFORMS 1 AND 4), TISSUE SPECIFICITY.		VSP_004728	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	245 – 319	75	Missing in isoform 3. Curated		VSP_004729	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	638 – 666	29	Missing in isoform 5. Curated		VSP_053718	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	751 – 760	10	KEQAIWKHPQ → RFPIKEKRKP in isoform 2. Curated		VSP_004730
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	761 – 805	45	Missing in isoform 2. Curated		VSP_004731	Add BLAST

Sequence databases

Genome annotation databases

Polymorphism databases

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - Coding sequence diversityⁱ

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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry

Protein family/group databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "Identification of PKDL, a novel polycystic kidney disease 2-like gene whose murine homologue is deleted in mice with kidney and retinal defects."
   Nomura H., Turco A.E., Pei Y., Kalaydjieva L., Schiavello T., Weremowicz S., Ji W., Morton C.C., Meisler M., Reeders S.T., Zhou J.
   J. Biol. Chem. 273:25967-25973(1998) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT ILE-393.
   Tissue: Retina.
   
2. "The human polycystic kidney disease 2-like (PKDL) gene: exon/intron structure and evidence for a novel splicing mechanism."
   Guo L., Chen M., Basora N., Zhou J.
   Mamm. Genome 11:46-50(2000) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4).
3. "The DNA sequence and comparative analysis of human chromosome 10."
   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.

   , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
   Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
4. Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R.

   , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
   The MGC Project Team
   Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
   Tissue: Brain.
   
6. "Identification of PKD2L, a human PKD2-related gene: tissue-specific expression and mapping to chromosome 10q25."
   Wu G., Hayashi T., Park J.-H., Dixit M., Reynolds D.M., Li L., Maeda Y., Cai Y., Coca-Prados M., Somlo S.
   Genomics 54:564-568(1998) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 96-805 (ISOFORM 1).
   Tissue: Retina.
   
7. "Genes homologous to the autosomal dominant polycystic kidney disease genes (PKD1 and PKD2)."
   Veldhuisen B., Spruit L., Dauwerse H.G., Breuning M.H., Peters D.J.M.
   Eur. J. Hum. Genet. 7:860-872(1999) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-805 (ISOFORMS 1 AND 4), TISSUE SPECIFICITY.
   Tissue: Testis.
   
8. "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]
   Cited for: FUNCTION.
9. "Polycystin channels and kidney disease."
   Stayner C., Zhou J.
   Trends Pharmacol. Sci. 22:543-546(2001) [PubMed] [Europe PMC] [Abstract]
   Cited for: REVIEW.
10. "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]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 2 AND 5).
11. "Off-response property of an acid-activated cation channel complex PKD1L3-PKD2L1."
    Inada H., Kawabata F., Ishimaru Y., Fushiki T., Matsunami H., Tominaga M.
    EMBO Rep. 9:690-697(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION.
12. "Acetic acid activates PKD1L3-PKD2L1 channel--a candidate sour taste receptor."
    Ishii S., Misaka T., Kishi M., Kaga T., Ishimaru Y., Abe K.
    Biochem. Biophys. Res. Commun. 385:346-350(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
13. "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]
    Cited for: FUNCTION.
14. "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]
    Cited for: SUBUNIT, CALCIUM-BINDING.
15. "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."
    Ishimaru Y., Katano Y., Yamamoto K., Akiba M., Misaka T., Roberts R.W., Asakura T., Matsunami H., Abe K.
    FASEB J. 24:4058-4067(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PKD1L1.
16. "The response of PKD1L3/PKD2L1 to acid stimuli is inhibited by capsaicin and its pungent analogs."
    Ishii S., Kurokawa A., Kishi M., Yamagami K., Okada S., Ishimaru Y., Misaka T.
    FEBS J. 279:1857-1870(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
17. "Receptor for activated C kinase 1 (RACK1) inhibits function of transient receptor potential (TRP)-type channel Pkd2L1 through physical interaction."
    Yang J., Wang Q., Zheng W., Tuli J., Li Q., Wu Y., Hussein S., Dai X.Q., Shafiei S., Li X.G., Shen P.Y., Tu J.C., Chen X.Z.
    J. Biol. Chem. 287:6551-6561(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GNB2L1.
18. "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]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PKD1L1, SUBCELLULAR LOCATION, MUTAGENESIS OF 523-GLU--GLU-525.
19. "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]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 699-737, SUBUNIT, CALCIUM-BINDING, MUTAGENESIS OF LEU-710; VAL-714; LEU-717; ILE-728; VAL-731 AND LEU-735.
20. "Molecular mechanism of the assembly of an acid-sensing receptor ion channel complex."
    Yu Y., Ulbrich M.H., Li M.H., Dobbins S., Zhang W.K., Tong L., Isacoff E.Y., Yang J.
    Nat. Commun. 3:1252-1252(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 699-743, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-523 AND ASP-525.

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Documents

1. Human chromosome 10
   Human chromosome 10: entries, gene names and cross-references to MIM
2. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
3. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
4. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
5. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
6. SIMILARITY comments
   Index of protein domains and families

External Data

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ