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Q9P0L9

- PK2L1_HUMAN

UniProt

Q9P0L9 - PK2L1_HUMAN

Protein

Polycystic kidney disease 2-like 1 protein

Gene

PKD2L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Pore-forming subunit of a ciliary calcium channel that controls calcium concentration within primary cilia without affecting cytoplasmic calcium concentration. Forms a heterodimer with PKD1L1 in primary cilia and forms a calcium-permeant ciliary channel that regulates sonic hedgehog/SHH signaling and GLI2 transcription. May act as a sour taste receptor by forming a calcium channel with PKD1L3 in gustatory cells; however, its contribution to sour taste perception is unclear in vivo and may be indirect.4 Publications

    Enzyme regulationi

    The calcium channel is gated following an off-response property by acid: gated open after the removal of acid stimulus, but not during acid application.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi646 – 65712Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. alpha-actinin binding Source: BHF-UCL
    2. calcium activated cation channel activity Source: BHF-UCL
    3. calcium-activated potassium channel activity Source: BHF-UCL
    4. calcium channel activity Source: UniProtKB
    5. calcium ion binding Source: UniProtKB
    6. cation channel activity Source: BHF-UCL
    7. cytoskeletal protein binding Source: UniProtKB
    8. identical protein binding Source: BHF-UCL
    9. muscle alpha-actinin binding Source: BHF-UCL
    10. protein binding Source: UniProtKB
    11. sodium channel activity Source: BHF-UCL
    12. sour taste receptor activity Source: Ensembl

    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
    6. protein homotrimerization Source: UniProtKB
    7. sensory perception of sour taste Source: UniProt
    8. smoothened signaling pathway Source: UniProtKB
    9. sodium ion transmembrane transport Source: BHF-UCL

    Keywords - Molecular functioni

    Calcium channel, Ion channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium

    Protein family/group databases

    TCDBi1.A.5.1.3. the polycystin cation channel (pcc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polycystic kidney disease 2-like 1 protein
    Alternative name(s):
    Polycystin-2 homolog
    Polycystin-2L1
    Polycystin-L
    Polycystin-L1
    Gene namesi
    Name:PKD2L1
    Synonyms:PKD2L, PKDL, TRPP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9011. PKD2L1.

    Subcellular locationi

    Cell projectioncilium membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum By similarity
    Note: Interaction with PKD1 or PKD1L3 is required for localization to the cell membrane.

    GO - Cellular componenti

    1. calcium channel complex Source: UniProtKB
    2. cell surface Source: Ensembl
    3. ciliary membrane Source: UniProtKB-SubCell
    4. endoplasmic reticulum Source: BHF-UCL
    5. integral component of membrane Source: UniProtKB
    6. intracellular membrane-bounded organelle Source: BHF-UCL
    7. membrane Source: UniProt
    8. nonmotile primary cilium Source: UniProtKB
    9. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cilium, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi523 – 5253DFD → AFA: Abolishes ion channel activity. 2 Publications
    Mutagenesisi523 – 5231D → Q: Increased permeability of dimethylamine and trimethylamine and decreased permeability of magnesium. 2 Publications
    Mutagenesisi525 – 5251D → K: Increased permeability of dimethylamine and trimethylamine and decreased permeability of magnesium. 2 Publications
    Mutagenesisi530 – 5301D → A: Does not affect ion channel activity. 1 Publication
    Mutagenesisi710 – 7101L → A: Abolishes homotrimer formation; when assocaited with A-714; A-717; A-728; A-731 and A-735. 2 Publications
    Mutagenesisi714 – 7141V → A: Abolishes homotrimer formation; when assocaited with A-710; A-717; A-728; A-731 and A-735. 2 Publications
    Mutagenesisi717 – 7171L → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-728; A-731 and A-735. 2 Publications
    Mutagenesisi728 – 7281I → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-731 and A-735. 2 Publications
    Mutagenesisi731 – 7311V → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-728 and A-735. 2 Publications
    Mutagenesisi735 – 7351L → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-728 and A-731. 2 Publications

    Organism-specific databases

    PharmGKBiPA33344.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 805805Polycystic kidney disease 2-like 1 proteinPRO_0000164360Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi505 – 5051N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9P0L9.
    PRIDEiQ9P0L9.

    Expressioni

    Tissue specificityi

    Expressed in adult heart, skeletal muscle, brain, spleen, testis, retina and liver. According to PubMed:9748274, expressed at high levels in fetal tissues, including kidney and liver, and down-regulated in adult tissues. According to PubMed:10602361, expressed in fetal brain, but not expressed in fetal lung, liver or kidney. Isoform 4 appears to be expressed only in transformed lymphoblasts.2 Publications

    Gene expression databases

    ArrayExpressiQ9P0L9.
    BgeeiQ9P0L9.
    CleanExiHS_PKD2L1.
    GenevestigatoriQ9P0L9.

    Organism-specific databases

    HPAiCAB022621.

    Interactioni

    Subunit structurei

    Homotrimer; trimerization is independent of calcium-binding. Calcium channels are probably composed of 3 subunit of PKD2L1 and 1 subunit of some PKD1 protein (PKD1, PKD1L1, PKD1L2 or PKDL3). Interacts with PKD1. Interacts with PKD1L1; to form ciliary calcium channel. Interacts with PKD1L3, to form putative sour taste receptor. Interacts with GNB2L1; inhibits the channel activity possibly by impairing localization to the cell membrane.6 Publications

    Protein-protein interaction databases

    BioGridi114499. 2 interactions.
    IntActiQ9P0L9. 1 interaction.
    MINTiMINT-3973148.
    STRINGi9606.ENSP00000325296.

    Structurei

    Secondary structure

    1
    805
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi704 – 73128
    Helixi734 – 7418

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3TE3X-ray2.69A/B/C/D/E/F699-737[»]
    4GIFX-ray2.80A699-743[»]
    ProteinModelPortaliQ9P0L9.
    SMRiQ9P0L9. Positions 597-675, 699-736.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 103103CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini125 – 313189ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini335 – 34713CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini369 – 38416ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini406 – 47671CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini498 – 53942ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini561 – 805245CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei104 – 12421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei314 – 33421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei348 – 36821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei385 – 40521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei477 – 49721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei540 – 56021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini633 – 66836EF-handAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni704 – 76360Required for protein homotrimerizationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili650 – 68637Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi195 – 20713Polycystin motifAdd
    BLAST

    Domaini

    The EF-hand domain probably mediates calcium-binding. It is not required for channel activation (PubMed:11959145).1 Publication

    Sequence similaritiesi

    Belongs to the polycystin family.Curated
    Contains 1 EF-hand domain.Curated

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG325704.
    HOGENOMiHOG000230858.
    HOVERGENiHBG014945.
    InParanoidiQ9P0L9.
    KOiK04990.
    OMAiFSTFVKC.
    OrthoDBiEOG7N8ZTW.
    PhylomeDBiQ9P0L9.
    TreeFamiTF316484.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR013122. PKD1_2_channel.
    IPR003915. PKD_2.
    [Graphical view]
    PfamiPF08016. PKD_channel. 1 hit.
    [Graphical view]
    PRINTSiPR01433. POLYCYSTIN2.

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q9P0L9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNAVGSPEGQ ELQKLGSGAW DNPAYSGPPS PHGTLRVCTI SSTGPLQPQP    50
    KKPEDEPQET AYRTQVSSCC LHICQGIRGL WGTTLTENTA ENRELYIKTT 100
    LRELLVYIVF LVDICLLTYG MTSSSAYYYT KVMSELFLHT PSDTGVSFQA 150
    ISSMADFWDF AQGPLLDSLY WTKWYNNQSL GHGSHSFIYY ENMLLGVPRL 200
    RQLKVRNDSC VVHEDFREDI LSCYDVYSPD KEEQLPFGPF NGTAWTYHSQ 250
    DELGGFSHWG RLTSYSGGGY YLDLPGSRQG SAEALRALQE GLWLDRGTRV 300
    VFIDFSVYNA NINLFCVLRL VVEFPATGGA IPSWQIRTVK LIRYVSNWDF 350
    FIVGCEVIFC VFIFYYVVEE ILELHIHRLR YLSSIWNILD LVVILLSIVA 400
    VGFHIFRTLE VNRLMGKLLQ QPNTYADFEF LAFWQTQYNN MNAVNLFFAW 450
    IKIFKYISFN KTMTQLSSTL ARCAKDILGF AVMFFIVFFA YAQLGYLLFG 500
    TQVENFSTFI KCIFTQFRII LGDFDYNAID NANRILGPAY FVTYVFFVFF 550
    VLLNMFLAII NDTYSEVKEE LAGQKDELQL SDLLKQGYNK TLLRLRLRKE 600
    RVSDVQKVLQ GGEQEIQFED FTNTLRELGH AEHEITELTA TFTKFDRDGN 650
    RILDEKEQEK MRQDLEEERV ALNTEIEKLG RSIVSSPQGK SGPEAARAGG 700
    WVSGEEFYML TRRVLQLETV LEGVVSQIDA VGSKLKMLER KGWLAPSPGV 750
    KEQAIWKHPQ PAPAVTPDPW GVQGGQESEV PYKREEEALE ERRLSRGEIP 800
    TLQRS 805
    Length:805
    Mass (Da):91,982
    Last modified:October 1, 2000 - v1
    Checksum:i3714C07F4B71F9C6
    GO
    Isoform 2 (identifier: Q9P0L9-2) [UniParc]FASTAAdd to Basket

    Also known as: PKDLdel15, PCL-TS, Testis isoform

    The sequence of this isoform differs from the canonical sequence as follows:
         751-760: KEQAIWKHPQ → RFPIKEKRKP
         761-805: Missing.

    Show »
    Length:760
    Mass (Da):86,988
    Checksum:i203D20F881C40055
    GO
    Isoform 3 (identifier: Q9P0L9-3) [UniParc]FASTAAdd to Basket

    Also known as: PKDLdel5

    The sequence of this isoform differs from the canonical sequence as follows:
         245-319: Missing.

    Show »
    Length:730
    Mass (Da):83,511
    Checksum:i02ABA835A71B32AD
    GO
    Isoform 4 (identifier: Q9P0L9-4) [UniParc]FASTAAdd to Basket

    Also known as: PKDLdel456

    The sequence of this isoform differs from the canonical sequence as follows:
         225-344: Missing.

    Note: Unusual intron exon spliced junction.

    Show »
    Length:685
    Mass (Da):78,520
    Checksum:iE805D32F37E6F54E
    GO
    Isoform 5 (identifier: Q9P0L9-5) [UniParc]FASTAAdd to Basket

    Also known as: PCL-LV, Liver isoform

    The sequence of this isoform differs from the canonical sequence as follows:
         638-666: Missing.

    Show »
    Length:776
    Mass (Da):88,472
    Checksum:i2EC2917E99DFF104
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131Q → H in AAD41638. (PubMed:9748274)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti278 – 2781R → Q.
    Corresponds to variant rs17112895 [ dbSNP | Ensembl ].
    VAR_050555
    Natural varianti378 – 3781R → W.
    Corresponds to variant rs7909153 [ dbSNP | Ensembl ].
    VAR_050556
    Natural varianti393 – 3931V → I.1 Publication
    Corresponds to variant rs2278842 [ dbSNP | Ensembl ].
    VAR_024569
    Natural varianti681 – 6811R → L.
    Corresponds to variant rs6584356 [ dbSNP | Ensembl ].
    VAR_024570
    Natural varianti788 – 7881A → D.
    Corresponds to variant rs12782963 [ dbSNP | Ensembl ].
    VAR_050557

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei225 – 344120Missing in isoform 4. 1 PublicationVSP_004728Add
    BLAST
    Alternative sequencei245 – 31975Missing in isoform 3. CuratedVSP_004729Add
    BLAST
    Alternative sequencei638 – 66629Missing in isoform 5. CuratedVSP_053718Add
    BLAST
    Alternative sequencei751 – 76010KEQAIWKHPQ → RFPIKEKRKP in isoform 2. CuratedVSP_004730
    Alternative sequencei761 – 80545Missing in isoform 2. CuratedVSP_004731Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF073481 mRNA. Translation: AAD41638.1.
    AF153474
    , AF153459, AF153460, AF153461, AF153462, AF153463, AF153464, AF153465, AF153466, AF153467, AF153468, AF153469, AF153470, AF153471, AF153472, AF153473 Genomic DNA. Translation: AAF28108.1.
    AL139819 Genomic DNA. Translation: CAH72822.1.
    CH471066 Genomic DNA. Translation: EAW49833.1.
    BC025665 mRNA. Translation: AAH25665.1.
    AF094827 mRNA. Translation: AAD08695.1.
    AF053316 mRNA. Translation: AAD51859.1.
    CCDSiCCDS7492.1. [Q9P0L9-1]
    RefSeqiNP_001240766.1. NM_001253837.1.
    NP_057196.2. NM_016112.2. [Q9P0L9-1]
    UniGeneiHs.159241.

    Genome annotation databases

    EnsembliENST00000318222; ENSP00000325296; ENSG00000107593. [Q9P0L9-1]
    GeneIDi9033.
    KEGGihsa:9033.
    UCSCiuc001kqx.1. human. [Q9P0L9-1]

    Polymorphism databases

    DMDMi23821938.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF073481 mRNA. Translation: AAD41638.1 .
    AF153474
    , AF153459 , AF153460 , AF153461 , AF153462 , AF153463 , AF153464 , AF153465 , AF153466 , AF153467 , AF153468 , AF153469 , AF153470 , AF153471 , AF153472 , AF153473 Genomic DNA. Translation: AAF28108.1 .
    AL139819 Genomic DNA. Translation: CAH72822.1 .
    CH471066 Genomic DNA. Translation: EAW49833.1 .
    BC025665 mRNA. Translation: AAH25665.1 .
    AF094827 mRNA. Translation: AAD08695.1 .
    AF053316 mRNA. Translation: AAD51859.1 .
    CCDSi CCDS7492.1. [Q9P0L9-1 ]
    RefSeqi NP_001240766.1. NM_001253837.1.
    NP_057196.2. NM_016112.2. [Q9P0L9-1 ]
    UniGenei Hs.159241.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3TE3 X-ray 2.69 A/B/C/D/E/F 699-737 [» ]
    4GIF X-ray 2.80 A 699-743 [» ]
    ProteinModelPortali Q9P0L9.
    SMRi Q9P0L9. Positions 597-675, 699-736.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114499. 2 interactions.
    IntActi Q9P0L9. 1 interaction.
    MINTi MINT-3973148.
    STRINGi 9606.ENSP00000325296.

    Chemistry

    ChEMBLi CHEMBL1628480.
    GuidetoPHARMACOLOGYi 505.

    Protein family/group databases

    TCDBi 1.A.5.1.3. the polycystin cation channel (pcc) family.

    Polymorphism databases

    DMDMi 23821938.

    Proteomic databases

    PaxDbi Q9P0L9.
    PRIDEi Q9P0L9.

    Protocols and materials databases

    DNASUi 9033.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318222 ; ENSP00000325296 ; ENSG00000107593 . [Q9P0L9-1 ]
    GeneIDi 9033.
    KEGGi hsa:9033.
    UCSCi uc001kqx.1. human. [Q9P0L9-1 ]

    Organism-specific databases

    CTDi 9033.
    GeneCardsi GC10M102037.
    HGNCi HGNC:9011. PKD2L1.
    HPAi CAB022621.
    MIMi 604532. gene.
    neXtProti NX_Q9P0L9.
    PharmGKBi PA33344.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG325704.
    HOGENOMi HOG000230858.
    HOVERGENi HBG014945.
    InParanoidi Q9P0L9.
    KOi K04990.
    OMAi FSTFVKC.
    OrthoDBi EOG7N8ZTW.
    PhylomeDBi Q9P0L9.
    TreeFami TF316484.

    Miscellaneous databases

    GeneWikii PKD2L1.
    GenomeRNAii 9033.
    NextBioi 33843.
    PROi Q9P0L9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P0L9.
    Bgeei Q9P0L9.
    CleanExi HS_PKD2L1.
    Genevestigatori Q9P0L9.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR013122. PKD1_2_channel.
    IPR003915. PKD_2.
    [Graphical view ]
    Pfami PF08016. PKD_channel. 1 hit.
    [Graphical view ]
    PRINTSi PR01433. POLYCYSTIN2.
    ProtoNeti Search...

    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. 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. 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.

    Entry informationi

    Entry nameiPK2L1_HUMAN
    AccessioniPrimary (citable) accession number: Q9P0L9
    Secondary accession number(s): O75972
    , Q5W039, Q9UP35, Q9UPA2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    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

    Dasty 3