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Q9P0L9

- PK2L1_HUMAN

UniProt

Q9P0L9 - PK2L1_HUMAN

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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

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. sodium channel activity Source: BHF-UCL
  11. 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
Complete GO annotation...

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. endoplasmic reticulum Source: BHF-UCL
  4. integral component of membrane Source: UniProtKB
  5. intracellular membrane-bounded organelle Source: BHF-UCL
  6. membrane Source: UniProt
  7. nonmotile primary cilium Source: UniProtKB
  8. plasma membrane Source: UniProtKB
Complete GO annotation...

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

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

BgeeiQ9P0L9.
CleanExiHS_PKD2L1.
ExpressionAtlasiQ9P0L9. baseline and differential.
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 – 73128Combined sources
Helixi734 – 7418Combined sources

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 477-563, 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.
GeneTreeiENSGT00700000104221.
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

        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
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 477-563, 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 GC10M102047.
HGNCi HGNC:9011. PKD2L1.
HPAi CAB022621.
MIMi 604532. gene.
neXtProti NX_Q9P0L9.
PharmGKBi PA33344.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG325704.
GeneTreei ENSGT00700000104221.
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

Bgeei Q9P0L9.
CleanExi HS_PKD2L1.
ExpressionAtlasi Q9P0L9. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 126 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

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