Q9P0L9 (PK2L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	805 AA.
Sequence status	Complete.
Protein existence	Evidence 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 projection › cilium 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 process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Cell projection Cilium Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Calcium channel Ion channel
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cation 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_component	calcium 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_function	alpha-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 805

805

Polycystic kidney disease 2-like 1 protein

PRO_0000164360

Regions

Topological domain

1 – 103

103

Cytoplasmic Potential

Transmembrane

104 – 124

21

Helical; Potential

Topological domain

125 – 313

189

Extracellular Potential

Transmembrane

314 – 334

21

Helical; Potential

Topological domain

335 – 347

13

Cytoplasmic Potential

Transmembrane

348 – 368

21

Helical; Potential

Topological domain

369 – 384

16

Extracellular Potential

Transmembrane

385 – 405

21

Helical; Potential

Topological domain

406 – 476

71

Cytoplasmic Potential

Transmembrane

477 – 497

21

Helical; Potential

Topological domain

498 – 539

42

Extracellular Potential

Transmembrane

540 – 560

21

Helical; Potential

Topological domain

561 – 805

245

Cytoplasmic Potential

Domain

633 – 668

36

EF-hand

Calcium binding

646 – 657

12

Potential

Region

704 – 763

60

Required for protein homotrimerization

Coiled coil

650 – 686

37

Potential

Motif

195 – 207

13

Polycystin motif

Amino acid modifications

Glycosylation

177

1

N-linked (GlcNAc...) Potential

Glycosylation

207

1

N-linked (GlcNAc...) Potential

Glycosylation

241

1

N-linked (GlcNAc...) Potential

Glycosylation

505

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

225 – 344

120

Missing in isoform 4.

VSP_004728

Alternative sequence

245 – 319

75

Missing in isoform 3.

VSP_004729

Alternative sequence

638 – 666

29

Missing in isoform 5.

VSP_053718

Alternative sequence

751 – 760

10

KEQAIWKHPQ → RFPIKEKRKP in isoform 2.

VSP_004730

Alternative sequence

761 – 805

45

Missing in isoform 2.

VSP_004731

Natural variant

278

1

R → Q.
Corresponds to variant rs17112895 [ dbSNP | Ensembl ].

VAR_050555

Natural variant

378

1

R → W.
Corresponds to variant rs7909153 [ dbSNP | Ensembl ].

VAR_050556

Natural variant

393

1

V → I. Ref.1
Corresponds to variant rs2278842 [ dbSNP | Ensembl ].

VAR_024569

Natural variant

681

1

R → L.
Corresponds to variant rs6584356 [ dbSNP | Ensembl ].

VAR_024570

Natural variant

788

1

A → D.
Corresponds to variant rs12782963 [ dbSNP | Ensembl ].

VAR_050557

Experimental info

Mutagenesis

523 – 525

3

DFD → AFA: Abolishes ion channel activity. Ref.18 Ref.20

Mutagenesis

523

1

D → Q: Increased permeability of dimethylamine and trimethylamine and decreased permeability of magnesium. Ref.20

Mutagenesis

525

1

D → K: Increased permeability of dimethylamine and trimethylamine and decreased permeability of magnesium. Ref.20

Mutagenesis

530

1

D → A: Does not affect ion channel activity.

Mutagenesis

710

1

L → A: Abolishes homotrimer formation; when assocaited with A-714; A-717; A-728; A-731 and A-735. Ref.19

Mutagenesis

714

1

V → A: Abolishes homotrimer formation; when assocaited with A-710; A-717; A-728; A-731 and A-735. Ref.19

Mutagenesis

717

1

L → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-728; A-731 and A-735. Ref.19

Mutagenesis

728

1

I → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-731 and A-735. Ref.19

Mutagenesis

731

1

V → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-728 and A-735. Ref.19

Mutagenesis

735

1

L → A: Abolishes homotrimer formation; when assocaited with A-710; A-714; A-717; A-728 and A-731. Ref.19

Sequence conflict

13

1

Q → H in AAD41638. Ref.1

Secondary structure

1

.

.

.

.

.

805

Helix Strand Turn

Details...

Helix

704 – 731

28

Helix

734 – 741

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 3714C07F4B71F9C6	FASTA	805	91,982
	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
	Isoform 2 (PKDLdel15) (PCL-TS) (Testis isoform) [UniParc]. Checksum: 203D20F881C40055	FASTA	760	86,988
	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 LEGVVSQIDA VGSKLKMLER KGWLAPSPGV RFPIKEKRKP
	Isoform 3 (PKDLdel5) [UniParc]. Checksum: 02ABA835A71B32AD	FASTA	730	83,511
	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 NGTALVVEFP ATGGAIPSWQ IRTVKLIRYV SNWDFFIVGC EVIFCVFIFY YVVEEILELH 310 320 330 340 350 360 IHRLRYLSSI WNILDLVVIL LSIVAVGFHI FRTLEVNRLM GKLLQQPNTY ADFEFLAFWQ 370 380 390 400 410 420 TQYNNMNAVN LFFAWIKIFK YISFNKTMTQ LSSTLARCAK DILGFAVMFF IVFFAYAQLG 430 440 450 460 470 480 YLLFGTQVEN FSTFIKCIFT QFRIILGDFD YNAIDNANRI LGPAYFVTYV FFVFFVLLNM 490 500 510 520 530 540 FLAIINDTYS EVKEELAGQK DELQLSDLLK QGYNKTLLRL RLRKERVSDV QKVLQGGEQE 550 560 570 580 590 600 IQFEDFTNTL RELGHAEHEI TELTATFTKF DRDGNRILDE KEQEKMRQDL EEERVALNTE 610 620 630 640 650 660 IEKLGRSIVS SPQGKSGPEA ARAGGWVSGE EFYMLTRRVL QLETVLEGVV SQIDAVGSKL 670 680 690 700 710 720 KMLERKGWLA PSPGVKEQAI WKHPQPAPAV TPDPWGVQGG QESEVPYKRE EEALEERRLS 730 RGEIPTLQRS
	Isoform 4 (PKDLdel456) [UniParc]. Checksum: E805D32F37E6F54E	FASTA	685	78,520
	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 LSCYVSNWDF FIVGCEVIFC 250 260 270 280 290 300 VFIFYYVVEE ILELHIHRLR YLSSIWNILD LVVILLSIVA VGFHIFRTLE VNRLMGKLLQ 310 320 330 340 350 360 QPNTYADFEF LAFWQTQYNN MNAVNLFFAW IKIFKYISFN KTMTQLSSTL ARCAKDILGF 370 380 390 400 410 420 AVMFFIVFFA YAQLGYLLFG TQVENFSTFI KCIFTQFRII LGDFDYNAID NANRILGPAY 430 440 450 460 470 480 FVTYVFFVFF VLLNMFLAII NDTYSEVKEE LAGQKDELQL SDLLKQGYNK TLLRLRLRKE 490 500 510 520 530 540 RVSDVQKVLQ GGEQEIQFED FTNTLRELGH AEHEITELTA TFTKFDRDGN RILDEKEQEK 550 560 570 580 590 600 MRQDLEEERV ALNTEIEKLG RSIVSSPQGK SGPEAARAGG WVSGEEFYML TRRVLQLETV 610 620 630 640 650 660 LEGVVSQIDA VGSKLKMLER KGWLAPSPGV KEQAIWKHPQ PAPAVTPDPW GVQGGQESEV 670 680 PYKREEEALE ERRLSRGEIP TLQRS
	Isoform 5 (PCL-LV) (Liver isoform) [UniParc]. Checksum: 2EC2917E99DFF104	FASTA	776	88,472
	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 AEHEITEEER VALNTEIEKL GRSIVSSPQG 670 680 690 700 710 720 KSGPEAARAG GWVSGEEFYM LTRRVLQLET VLEGVVSQID AVGSKLKMLE RKGWLAPSPG 730 740 750 760 770 VKEQAIWKHP QPAPAVTPDP WGVQGGQESE VPYKREEEAL EERRLSRGEI PTLQRS

References

	« Hide 'large scale' referencesShow '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. , 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

CCDS

CCDS7492.1. [Q9P0L9-1]

RefSeq

NP_001240766.1. NM_001253837.1.
NP_057196.2. NM_016112.2. [Q9P0L9-1]

UniGene

Hs.159241.

3D structure databases

PDBe
RCSB-PDB
PDBj

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	[»]

ProteinModelPortal

Q9P0L9.

SMR

Q9P0L9. Positions 597-675, 699-736.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

114499. 2 interactions.

IntAct

Q9P0L9. 1 interaction.

MINT

MINT-3973148.

STRING

9606.ENSP00000325296.

Chemistry

ChEMBL

CHEMBL1628480.

GuidetoPHARMACOLOGY

505.

Protein family/group databases

TCDB

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

Polymorphism databases

DMDM

23821938.

Proteomic databases

PaxDb

Q9P0L9.

PRIDE

Q9P0L9.

Protocols and materials databases

DNASU

9033.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000318222; ENSP00000325296; ENSG00000107593. [Q9P0L9-1]
ENST00000338519; ENSP00000345068; ENSG00000107593. [Q9P0L9-3]
ENST00000353274; ENSP00000266049; ENSG00000107593. [Q9P0L9-2]

GeneID

9033.

KEGG

hsa:9033.

UCSC

uc001kqx.1. human. [Q9P0L9-1]

Organism-specific databases

CTD

9033.

GeneCards

GC10M102037.

HGNC

HGNC:9011. PKD2L1.

HPA

CAB022621.

MIM

604532. gene.

neXtProt

NX_Q9P0L9.

PharmGKB

PA33344.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG325704.

HOGENOM

HOG000230858.

HOVERGEN

HBG014945.

InParanoid

Q9P0L9.

KO

K04990.

OMA

FSTFVKC.

OrthoDB

EOG7N8ZTW.

PhylomeDB

Q9P0L9.

TreeFam

TF316484.

Gene expression databases

ArrayExpress

Q9P0L9.

Bgee

Q9P0L9.

CleanEx

HS_PKD2L1.

Genevestigator

Q9P0L9.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.

InterPro

IPR011992. EF-hand-dom_pair.
IPR013122. PKD1_2_channel.
IPR003915. PKD_2.
[Graphical view]

Pfam

PF08016. PKD_channel. 1 hit.
[Graphical view]

PRINTS

PR01433. POLYCYSTIN2.

ProtoNet

Search...

Other

GeneWiki

PKD2L1.

GenomeRNAi

9033.

NextBio

33843.

PRO

Q9P0L9.

SOURCE

Search...

Entry information

Entry name

PK2L1_HUMAN

Accession

Primary (citable) accession number: Q9P0L9
Secondary accession number(s): O75972 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.