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Q9P0L9 (PK2L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polycystic kidney disease 2-like 1 protein
Alternative name(s):
Polycystin-2 homolog
Polycystin-2L1
Polycystin-L
Polycystin-L1
Gene names
Name:PKD2L1
Synonyms:PKD2L, PKDL, TRPP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length805 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.13 Ref.18 Ref.20

Enzyme regulation

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. Ref.11 Ref.12 Ref.16

Subunit structure

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. Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20

Subcellular location

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. Ref.11 Ref.15 Ref.18 Ref.20

Tissue specificity

Expressed in adult heart, skeletal muscle, brain, spleen, testis, retina and liver. According to Ref.1, expressed at high levels in fetal tissues, including kidney and liver, and down-regulated in adult tissues. According to Ref.7, expressed in fetal brain, but not expressed in fetal lung, liver or kidney. Isoform 4 appears to be expressed only in transformed lymphoblasts. Ref.1 Ref.7

Domain

The EF-hand domain probably mediates calcium-binding. It is not required for channel activation (Ref.10).

Sequence similarities

Belongs to the polycystin family.

Contains 1 EF-hand domain.

Caution

PKD1L3 and PKD2L1 have been defined as sour taste receptor in gustatory cells based on a number of indirect evidences in mouse. Some data confirm this hypothesis in human: in 2 patients with sour ageusia that are unresponsive to sour stimuli, but show normal responses to bitter, sweet, and salty stimuli, expression of PKD1L3 and PKD2L1 is absent in the anterior part of the tongue (Ref.13). However, a number of experiments have recently shown that the sour taste receptor activity is probably indirect.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentCell membrane
Cell projection
Cilium
Endoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionCalcium channel
Ion channel
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcation transport

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to acidity

Inferred from sequence or structural similarity. Source: BHF-UCL

detection of chemical stimulus involved in sensory perception of sour taste

Inferred from sequence or structural similarity. Source: BHF-UCL

detection of mechanical stimulus

Inferred from Biological aspect of Ancestor. Source: RefGenome

potassium ion transmembrane transport

Inferred from direct assay Ref.8. Source: BHF-UCL

protein homotrimerization

Inferred from direct assay Ref.19. Source: UniProtKB

sensory perception of sour taste

Inferred from mutant phenotype Ref.13. Source: UniProt

smoothened signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

sodium ion transmembrane transport

Inferred from direct assay Ref.8. Source: BHF-UCL

   Cellular_componentcalcium channel complex

Inferred from direct assay Ref.18. Source: UniProtKB

cell surface

Inferred from electronic annotation. Source: Ensembl

ciliary membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: BHF-UCL

integral component of membrane

Non-traceable author statement Ref.6. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 17944866. Source: BHF-UCL

membrane

Inferred from direct assay Ref.13. Source: UniProt

nonmotile primary cilium

Inferred from direct assay Ref.18. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.15. Source: UniProtKB

   Molecular_functionalpha-actinin binding

Inferred from physical interaction PubMed 17944866. Source: BHF-UCL

calcium activated cation channel activity

Inferred from direct assay Ref.8Ref.10. Source: BHF-UCL

calcium channel activity

Inferred from direct assay Ref.18. Source: UniProtKB

calcium ion binding

Inferred from direct assay Ref.19. Source: UniProtKB

calcium-activated potassium channel activity

Inferred from direct assay Ref.8. Source: BHF-UCL

cation channel activity

Inferred from direct assay PubMed 17944866. Source: BHF-UCL

cytoskeletal protein binding

Inferred from physical interaction PubMed 12809519. Source: UniProtKB

identical protein binding

Inferred from sequence or structural similarity. Source: BHF-UCL

muscle alpha-actinin binding

Inferred from physical interaction PubMed 17944866. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 12525172Ref.15Ref.18. Source: UniProtKB

sodium channel activity

Inferred from direct assay Ref.8. Source: BHF-UCL

sour taste receptor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9P0L9-1)

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.
Isoform 2 (identifier: Q9P0L9-2)

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.
Isoform 3 (identifier: Q9P0L9-3)

Also known as: PKDLdel5;

The sequence of this isoform differs from the canonical sequence as follows:
     245-319: Missing.
Isoform 4 (identifier: Q9P0L9-4)

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.
Isoform 5 (identifier: Q9P0L9-5)

Also known as: PCL-LV; Liver isoform;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 805805Polycystic kidney disease 2-like 1 protein
PRO_0000164360

Regions

Topological domain1 – 103103Cytoplasmic Potential
Transmembrane104 – 12421Helical; Potential
Topological domain125 – 313189Extracellular Potential
Transmembrane314 – 33421Helical; Potential
Topological domain335 – 34713Cytoplasmic Potential
Transmembrane348 – 36821Helical; Potential
Topological domain369 – 38416Extracellular Potential
Transmembrane385 – 40521Helical; Potential
Topological domain406 – 47671Cytoplasmic Potential
Transmembrane477 – 49721Helical; Potential
Topological domain498 – 53942Extracellular Potential
Transmembrane540 – 56021Helical; Potential
Topological domain561 – 805245Cytoplasmic Potential
Domain633 – 66836EF-hand
Calcium binding646 – 65712 Potential
Region704 – 76360Required for protein homotrimerization
Coiled coil650 – 68637 Potential
Motif195 – 20713Polycystin motif

Amino acid modifications

Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation5051N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence225 – 344120Missing in isoform 4.
VSP_004728
Alternative sequence245 – 31975Missing in isoform 3.
VSP_004729
Alternative sequence638 – 66629Missing in isoform 5.
VSP_053718
Alternative sequence751 – 76010KEQAIWKHPQ → RFPIKEKRKP in isoform 2.
VSP_004730
Alternative sequence761 – 80545Missing in isoform 2.
VSP_004731
Natural variant2781R → Q.
Corresponds to variant rs17112895 [ dbSNP | Ensembl ].
VAR_050555
Natural variant3781R → W.
Corresponds to variant rs7909153 [ dbSNP | Ensembl ].
VAR_050556
Natural variant3931V → I. Ref.1
Corresponds to variant rs2278842 [ dbSNP | Ensembl ].
VAR_024569
Natural variant6811R → L.
Corresponds to variant rs6584356 [ dbSNP | Ensembl ].
VAR_024570
Natural variant7881A → D.
Corresponds to variant rs12782963 [ dbSNP | Ensembl ].
VAR_050557

Experimental info

Mutagenesis523 – 5253DFD → AFA: Abolishes ion channel activity. Ref.18 Ref.20
Mutagenesis5231D → Q: Increased permeability of dimethylamine and trimethylamine and decreased permeability of magnesium. Ref.20
Mutagenesis5251D → K: Increased permeability of dimethylamine and trimethylamine and decreased permeability of magnesium. Ref.20
Mutagenesis5301D → A: Does not affect ion channel activity.
Mutagenesis7101L → A: Abolishes homotrimer formation; when assocaited with A-714; A-717; A-728; A-731 and A-735. Ref.19
Mutagenesis7141V → A: Abolishes homotrimer formation; when assocaited with A-710; A-717; A-728; A-731 and A-735. Ref.19
Mutagenesis7171L → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-728; A-731 and A-735. Ref.19
Mutagenesis7281I → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-731 and A-735. Ref.19
Mutagenesis7311V → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-728 and A-735. Ref.19
Mutagenesis7351L → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-728 and A-731. Ref.19
Sequence conflict131Q → H in AAD41638. Ref.1

Secondary structure

..... 805
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3714C07F4B71F9C6

FASTA80591,982
        10         20         30         40         50         60 
MNAVGSPEGQ ELQKLGSGAW DNPAYSGPPS PHGTLRVCTI SSTGPLQPQP KKPEDEPQET 

        70         80         90        100        110        120 
AYRTQVSSCC LHICQGIRGL WGTTLTENTA ENRELYIKTT LRELLVYIVF LVDICLLTYG 

       130        140        150        160        170        180 
MTSSSAYYYT KVMSELFLHT PSDTGVSFQA ISSMADFWDF AQGPLLDSLY WTKWYNNQSL 

       190        200        210        220        230        240 
GHGSHSFIYY ENMLLGVPRL RQLKVRNDSC VVHEDFREDI LSCYDVYSPD KEEQLPFGPF 

       250        260        270        280        290        300 
NGTAWTYHSQ DELGGFSHWG RLTSYSGGGY YLDLPGSRQG SAEALRALQE GLWLDRGTRV 

       310        320        330        340        350        360 
VFIDFSVYNA NINLFCVLRL VVEFPATGGA IPSWQIRTVK LIRYVSNWDF FIVGCEVIFC 

       370        380        390        400        410        420 
VFIFYYVVEE ILELHIHRLR YLSSIWNILD LVVILLSIVA VGFHIFRTLE VNRLMGKLLQ 

       430        440        450        460        470        480 
QPNTYADFEF LAFWQTQYNN MNAVNLFFAW IKIFKYISFN KTMTQLSSTL ARCAKDILGF 

       490        500        510        520        530        540 
AVMFFIVFFA YAQLGYLLFG TQVENFSTFI KCIFTQFRII LGDFDYNAID NANRILGPAY 

       550        560        570        580        590        600 
FVTYVFFVFF VLLNMFLAII NDTYSEVKEE LAGQKDELQL SDLLKQGYNK TLLRLRLRKE 

       610        620        630        640        650        660 
RVSDVQKVLQ GGEQEIQFED FTNTLRELGH AEHEITELTA TFTKFDRDGN RILDEKEQEK 

       670        680        690        700        710        720 
MRQDLEEERV ALNTEIEKLG RSIVSSPQGK SGPEAARAGG WVSGEEFYML TRRVLQLETV 

       730        740        750        760        770        780 
LEGVVSQIDA VGSKLKMLER KGWLAPSPGV KEQAIWKHPQ PAPAVTPDPW GVQGGQESEV 

       790        800 
PYKREEEALE ERRLSRGEIP TLQRS 

« Hide

Isoform 2 (PKDLdel15) (PCL-TS) (Testis isoform) [UniParc].

Checksum: 203D20F881C40055
Show »

FASTA76086,988
Isoform 3 (PKDLdel5) [UniParc].

Checksum: 02ABA835A71B32AD
Show »

FASTA73083,511
Isoform 4 (PKDLdel456) [UniParc].

Checksum: E805D32F37E6F54E
Show »

FASTA68578,520
Isoform 5 (PCL-LV) (Liver isoform) [UniParc].

Checksum: 2EC2917E99DFF104
Show »

FASTA77688,472

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF073481 mRNA. Translation: AAD41638.1.
AF153474 expand/collapse EMBL AC list , 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.
CCDSCCDS7492.1. [Q9P0L9-1]
RefSeqNP_001240766.1. NM_001253837.1.
NP_057196.2. NM_016112.2. [Q9P0L9-1]
UniGeneHs.159241.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TE3X-ray2.69A/B/C/D/E/F699-737[»]
4GIFX-ray2.80A699-743[»]
ProteinModelPortalQ9P0L9.
SMRQ9P0L9. Positions 597-675, 699-736.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114499. 2 interactions.
IntActQ9P0L9. 1 interaction.
MINTMINT-3973148.
STRING9606.ENSP00000325296.

Chemistry

ChEMBLCHEMBL1628480.
GuidetoPHARMACOLOGY505.

Protein family/group databases

TCDB1.A.5.1.3. the polycystin cation channel (pcc) family.

Polymorphism databases

DMDM23821938.

Proteomic databases

PaxDbQ9P0L9.
PRIDEQ9P0L9.

Protocols and materials databases

DNASU9033.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318222; ENSP00000325296; ENSG00000107593. [Q9P0L9-1]
ENST00000338519; ENSP00000345068; ENSG00000107593. [Q9P0L9-3]
ENST00000353274; ENSP00000266049; ENSG00000107593. [Q9P0L9-2]
GeneID9033.
KEGGhsa:9033.
UCSCuc001kqx.1. human. [Q9P0L9-1]

Organism-specific databases

CTD9033.
GeneCardsGC10M102037.
HGNCHGNC:9011. PKD2L1.
HPACAB022621.
MIM604532. gene.
neXtProtNX_Q9P0L9.
PharmGKBPA33344.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG325704.
HOGENOMHOG000230858.
HOVERGENHBG014945.
InParanoidQ9P0L9.
KOK04990.
OMAFSTFVKC.
OrthoDBEOG7N8ZTW.
PhylomeDBQ9P0L9.
TreeFamTF316484.

Gene expression databases

ArrayExpressQ9P0L9.
BgeeQ9P0L9.
CleanExHS_PKD2L1.
GenevestigatorQ9P0L9.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR013122. PKD1_2_channel.
IPR003915. PKD_2.
[Graphical view]
PfamPF08016. PKD_channel. 1 hit.
[Graphical view]
PRINTSPR01433. POLYCYSTIN2.
ProtoNetSearch...

Other

GeneWikiPKD2L1.
GenomeRNAi9033.
NextBio33843.
PROQ9P0L9.
SOURCESearch...

Entry information

Entry namePK2L1_HUMAN
AccessionPrimary (citable) accession number: Q9P0L9
Secondary accession number(s): O75972 expand/collapse secondary AC list , Q5W039, Q9UP35, Q9UPA2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM