Q13563 (PKD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polycystin-2

Alternative name(s):
Autosomal dominant polycystic kidney disease type II protein
Polycystic kidney disease 2 protein
Polycystwin
R48321

Gene names

Name:

PKD2

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	968 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium By similarity. PKD1 and PKD2 may function through a common signaling pathway that is necessary for normal tubulogenesis By similarity. Acts as a regulator of cilium length, together with PKD1 By similarity. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling By similarity. Functions as a calcium permeable cation channel.
Subunit structure	Forms homooligomers. Isoform 1 interacts with PKD1 while isoform 3 does not By similarity. PKD1 requires the presence of PKD2 for stable expression. Interacts with CD2AP. Interacts with HAX1. Interacts with NEK8 By similarity. Part of a complex containing AKAP5, ADCY5, ADCY6 and PDE4C By similarity. Ref.5 Ref.6 Ref.10
Subcellular location	Membrane; Multi-pass membrane protein Potential. Endoplasmic reticulum. Cell projection › cilium By similarity Ref.6.
Tissue specificity	Strongly expressed in ovary, fetal and adult kidney, testis, and small intestine. Not detected in peripheral leukocytes. Ref.1
Domain	The C-terminal coiled-coil domain binds calcium and undergoes a calcium-induced conformation change. It is implicated in oligomerization and the interaction with PKD1. Ref.10
Involvement in disease	Polycystic kidney disease 2 (PKD2) [MIM:613095]: A disorder characterized by progressive formation and enlargement of cysts in both kidneys, typically leading to end-stage renal disease in adult life. Cysts also occurs in the liver and other organs. It represents approximately 15% of the cases of autosomal dominant polycystic kidney disease. PKD2 is clinically milder than PKD1 but it has a deleterious impact on overall life expectancy. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20
Sequence similarities	Belongs to the polycystin family. Contains 1 EF-hand domain.

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell projection Cilium Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Ciliopathy Disease mutation
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Ion channel
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade Inferred from sequence or structural similarity. Source: BHF-UCL aorta development Inferred from expression pattern PubMed 11891195. Source: UniProtKB branching involved in ureteric bud morphogenesis Inferred from expression pattern PubMed 11891195. Source: UniProtKB cell cycle arrest Inferred from sequence or structural similarity. Source: BHF-UCL cellular response to fluid shear stress Inferred from mutant phenotype PubMed 19265036. Source: BHF-UCL cellular response to hydrostatic pressure Inferred from direct assay PubMed 16025301. Source: BHF-UCL cellular response to osmotic stress Inferred from direct assay PubMed 16025301. Source: BHF-UCL cellular response to reactive oxygen species Non-traceable author statement PubMed 18417208. Source: BHF-UCL centrosome duplication Non-traceable author statement PubMed 18725310. Source: BHF-UCL cytoplasmic sequestering of transcription factor Inferred from mutant phenotype PubMed 16311606. Source: BHF-UCL detection of mechanical stimulus Inferred from sequence or structural similarity. Source: BHF-UCL detection of nodal flow Inferred from sequence or structural similarity. Source: BHF-UCL determination of liver left/right asymmetry Inferred from mutant phenotype PubMed 21719175. Source: BHF-UCL embryonic placenta development Inferred from sequence or structural similarity. Source: BHF-UCL heart looping Inferred from mutant phenotype PubMed 21719175. Source: BHF-UCL mesonephric duct development Inferred from expression pattern PubMed 11891195. Source: UniProtKB metanephric S-shaped body morphogenesis Inferred from expression pattern PubMed 11891195. Source: UniProtKB metanephric ascending thin limb development Inferred from expression pattern PubMed 11891195. Source: UniProtKB metanephric cortex development Inferred from expression pattern PubMed 11891195. Source: UniProtKB metanephric cortical collecting duct development Inferred from expression pattern PubMed 11891195. Source: UniProtKB metanephric distal tubule development Inferred from expression pattern PubMed 11891195. Source: UniProtKB metanephric mesenchyme development Inferred from expression pattern PubMed 11891195. Source: UniProtKB metanephric part of ureteric bud development Inferred from expression pattern PubMed 11891195. Source: UniProtKB metanephric smooth muscle tissue development Inferred from expression pattern PubMed 11891195. Source: UniProtKB negative regulation of G1/S transition of mitotic cell cycle Inferred from mutant phenotype PubMed 16311606. Source: BHF-UCL negative regulation of cell proliferation Non-traceable author statement PubMed 18664456. Source: BHF-UCL negative regulation of ryanodine-sensitive calcium-release channel activity Inferred from sequence or structural similarity. Source: BHF-UCL neural tube development Inferred from expression pattern PubMed 11891195. Source: UniProtKB placenta blood vessel development Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cell cycle arrest Inferred from mutant phenotype PubMed 16311606. Source: BHF-UCL positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S Inferred from direct assay PubMed 16311606. Source: BHF-UCL positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Inferred from mutant phenotype PubMed 16223735. Source: BHF-UCL positive regulation of nitric oxide biosynthetic process Inferred from mutant phenotype PubMed 19265036. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 16311606. Source: BHF-UCL regulation of cAMP metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL regulation of calcium ion import Inferred from direct assay PubMed 11854751. Source: BHF-UCL release of sequestered calcium ion into cytosol Inferred from direct assay PubMed 11854751. Source: BHF-UCL renal artery morphogenesis Inferred from expression pattern PubMed 11891195. Source: UniProtKB renal tubule morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL spinal cord development Inferred from expression pattern PubMed 11891195. Source: UniProtKB
Cellular_component	basal cortex Inferred from direct assay PubMed 10770959. Source: BHF-UCL basal plasma membrane Inferred from direct assay PubMed 10770959. Source: BHF-UCL cell-cell junction Inferred from electronic annotation. Source: Compara cilium part Inferred from electronic annotation. Source: Compara integral to cytosolic side of endoplasmic reticulum membrane Inferred from direct assay PubMed 21044049. Source: BHF-UCL integral to lumenal side of endoplasmic reticulum membrane Inferred from direct assay PubMed 21044049. Source: BHF-UCL integral to plasma membrane Inferred from direct assay PubMed 21044049. Source: BHF-UCL lamellipodium Inferred from direct assay Ref.6. Source: BHF-UCL microtubule basal body Inferred from direct assay PubMed 15337773. Source: MGI mitotic spindle Inferred from direct assay PubMed 15123714. Source: BHF-UCL motile primary cilium Inferred from sequence or structural similarity. Source: BHF-UCL nonmotile primary cilium Inferred from sequence or structural similarity. Source: BHF-UCL polycystin complex Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	ATPase binding Inferred from sequence or structural similarity. Source: BHF-UCL actinin binding Inferred from direct assay PubMed 15843396. Source: BHF-UCL calcium ion binding Inferred from sequence or structural similarity. Source: BHF-UCL calcium-induced calcium release activity Inferred from direct assay PubMed 11854751. Source: BHF-UCL potassium channel activity Inferred from sequence or structural similarity. Source: BHF-UCL protein homodimerization activity Inferred from direct assay PubMed 9192675. Source: BHF-UCL voltage-gated calcium channel activity Inferred from direct assay PubMed 11252306PubMed 15692563. Source: BHF-UCL voltage-gated sodium channel activity Inferred from direct assay PubMed 11252306. Source: BHF-UCL
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q13563-1)

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: Q13563-2)

Also known as: delta6;

The sequence of this isoform differs from the canonical sequence as follows:
     476-483: CEIIFCFF → FICSSYGD
     484-968: Missing.

Isoform 3 (identifier: Q13563-3)

Also known as: delta7;

The sequence of this isoform differs from the canonical sequence as follows:
     517-572: Missing.

Isoform 4 (identifier: Q13563-4)

Also known as: delta9;

The sequence of this isoform differs from the canonical sequence as follows:
     633-646: IFTQFRIILGDINF → IICSWRSSMIRTLK
     647-968: Missing.

Isoform 5 (identifier: Q13563-5)

Also known as: delta12/13;

The sequence of this isoform differs from the canonical sequence as follows:
     748-841: Missing.

Note: Minor isoform.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 968

968

Polycystin-2

PRO_0000164356

Regions

Topological domain

1 – 223

223

Cytoplasmic Potential

Transmembrane

224 – 244

21

Helical; Potential

Topological domain

245 – 468

224

Extracellular Potential

Transmembrane

469 – 489

21

Helical; Potential

Topological domain

490 – 505

16

Cytoplasmic Potential

Transmembrane

506 – 526

21

Helical; Potential

Topological domain

527 – 550

24

Extracellular Potential

Transmembrane

551 – 571

21

Helical; Potential

Topological domain

572 – 598

27

Cytoplasmic Potential

Transmembrane

599 – 619

21

Helical; Potential

Topological domain

620 – 658

39

Extracellular Potential

Transmembrane

659 – 679

21

Helical; Potential

Topological domain

680 – 968

289

Cytoplasmic Potential

Domain

750 – 785

36

EF-hand

Calcium binding

763 – 774

12

Ref.10

Region

704 – 794

91

EF-hand domain

Region

803 – 822

20

Linker

Region

828 – 968

141

C-terminal coiled coil domain

Coiled coil

838 – 926

89

Potential

Motif

316 – 328

13

Polycystin motif

Compositional bias

95 – 107

13

Poly-Glu

Compositional bias

153 – 157

5

Poly-Arg

Amino acid modifications

Modified residue

812

1

Phosphoserine Ref.9

Glycosylation

299

1

N-linked (GlcNAc...) Potential

Glycosylation

305

1

N-linked (GlcNAc...) Potential

Glycosylation

328

1

N-linked (GlcNAc...) Potential

Glycosylation

362

1

N-linked (GlcNAc...) Potential

Glycosylation

375

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

476 – 483

8

CEIIFCFF → FICSSYGD in isoform 2.

VSP_042479

Alternative sequence

484 – 968

485

Missing in isoform 2.

VSP_042480

Alternative sequence

517 – 572

56

Missing in isoform 3.

VSP_042481

Alternative sequence

633 – 646

14

IFTQF…GDINF → IICSWRSSMIRTLK in isoform 4.

VSP_042482

Alternative sequence

647 – 968

322

Missing in isoform 4.

VSP_042483

Alternative sequence

748 – 841

94

Missing in isoform 5.

VSP_042484

Natural variant

24

1

P → L. Ref.15

VAR_058820

Natural variant

28

1

R → P Common polymorphism; possibly damaging. Ref.3 Ref.13 Ref.15 Ref.17 Ref.19
Corresponds to variant rs1805044 [ dbSNP | Ensembl ].

VAR_011072

Natural variant

190

1

A → T. Ref.19

VAR_058821

Natural variant

306

1

R → Q in PKD2. Ref.17

VAR_058822

Natural variant

322

1

R → Q in PKD2. Ref.18

VAR_058823

Natural variant

322

1

R → W in PKD2. Ref.15

VAR_058824

Natural variant

356

1

A → P in PKD2. Ref.13 Ref.16

VAR_011073

Natural variant

384

1

A → P in PKD2. Ref.20

VAR_064394

Natural variant

414

1

W → G in PKD2. Ref.11 Ref.16

VAR_009195

Natural variant

420

1

R → G in PKD2. Ref.17

VAR_058825

Natural variant

452

1

I → V.
Corresponds to variant rs1801612 [ dbSNP | Ensembl ].

VAR_014919

Natural variant

479

1

Missing in PKD2; somatic mutation. Ref.14

VAR_011074

Natural variant

482

1

F → C. Ref.19

VAR_058826

Natural variant

504 – 512

9

Missing in PKD2; somatic mutation.

VAR_011075

Natural variant

511

1

D → V in PKD2. Ref.12

VAR_058827

Natural variant

632

1

C → R in PKD2. Ref.16

VAR_058828

Natural variant

684

1

Missing in PKD2; somatic mutation. Ref.14

VAR_011076

Natural variant

800

1

M → L. Ref.15
Corresponds to variant rs2234917 [ dbSNP | Ensembl ].

VAR_058829

Natural variant

807

1

R → Q in PKD2. Ref.16

VAR_058830

Experimental info

Mutagenesis

771

1

T → A: Loss of calcium-binding site; when associated with A-774. Ref.10

Mutagenesis

774

1

E → A: Loss of calcium-binding site; when associated with A-771. Ref.10

Mutagenesis

842

1

L → P: Loss of protein solubility. Ref.10

Mutagenesis

846

1

V → E: Loss of protein solubility. Ref.10

Mutagenesis

849

1

M → K: Loss of protein solubility. Ref.10

Mutagenesis

853

1

I → P: Loss of protein solubility. Ref.10

Mutagenesis

856

1

I → K: Loss of protein solubility. Ref.10

Mutagenesis

863

1

V → E: Loss of protein solubility; when associated with K-849. Ref.10

Sequence conflict

45

1

G → R in AAC16004. Ref.2

Sequence conflict

449

1

G → V in AAC50933. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

968

Helix Strand Turn

Details...

Turn

730 – 734

5

Helix

738 – 744

7

Turn

745 – 747

3

Helix

752 – 762

11

Beta strand

763 – 766

4

Beta strand

767 – 771

5

Helix

773 – 777

5

Turn

781 – 783

3

Beta strand

793 – 795

3

Helix

836 – 894

59

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: F8D2E760EBEA8B47	FASTA	968	109,691
	10 20 30 40 50 60 MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR GLEIEMQRIR 70 80 90 100 110 120 QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE EEVEGEEGGM VVEMDVEWRP 130 140 150 160 170 180 GSRRSAASSA VSSVGARSRG LGGYHGAGHP SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL 190 200 210 220 230 240 EGQPPRVAWA ERLVRGLRGL WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG 250 260 270 280 290 300 MMSSNVYYYT RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 310 320 330 340 350 360 TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV SSEDRAPFGP 370 380 390 400 410 420 RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE ETAAQVASLK KNVWLDRGTR 430 440 450 460 470 480 ATFIDFSVYN ANINLFCVVR LLVEFPATGG VIPSWQFQPL KLIRYVTTFD FFLAACEIIF 490 500 510 520 530 540 CFFIFYYVVE EILEIRIHKL HYFRSFWNCL DVVIVVLSVV AIGINIYRTS NVEVLLQFLE 550 560 570 580 590 600 DQNTFPNFEH LAYWQIQFNN IAAVTVFFVW IKLFKFINFN RTMSQLSTTM SRCAKDLFGF 610 620 630 640 650 660 AIMFFIIFLA YAQLAYLVFG TQVDDFSTFQ ECIFTQFRII LGDINFAEIE EANRVLGPIY 670 680 690 700 710 720 FTTFVFFMFF ILLNMFLAII NDTYSEVKSD LAQQKAEMEL SDLIRKGYHK ALVKLKLKKN 730 740 750 760 770 780 TVDDISESLR QGGGKLNFDE LRQDLKGKGH TDAEIEAIFT KYDQDGDQEL TEHEHQQMRD 790 800 810 820 830 840 DLEKEREDLD LDHSSLPRPM SSRSFPRSLD DSEEDDDEDS GHSSRRRGSI SSGVSYEEFQ 850 860 870 880 890 900 VLVRRVDRME HSIGSIVSKI DAVIVKLEIM ERAKLKRREV LGRLLDGVAE DERLGRDSEI 910 920 930 940 950 960 HREQMERLVR EELERWESDD AASQISHGLG TPVGLNGQPR PRSSRPSSSQ STEGMEGAGG NGSSNVHV
	Isoform 2 (delta6) [UniParc]. Checksum: 6F4CC2DD18EEF56F	FASTA	483	53,686
	10 20 30 40 50 60 MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR GLEIEMQRIR 70 80 90 100 110 120 QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE EEVEGEEGGM VVEMDVEWRP 130 140 150 160 170 180 GSRRSAASSA VSSVGARSRG LGGYHGAGHP SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL 190 200 210 220 230 240 EGQPPRVAWA ERLVRGLRGL WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG 250 260 270 280 290 300 MMSSNVYYYT RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 310 320 330 340 350 360 TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV SSEDRAPFGP 370 380 390 400 410 420 RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE ETAAQVASLK KNVWLDRGTR 430 440 450 460 470 480 ATFIDFSVYN ANINLFCVVR LLVEFPATGG VIPSWQFQPL KLIRYVTTFD FFLAAFICSS YGD
	Isoform 3 (delta7) [UniParc]. Checksum: EDD0DB1BD7750772	FASTA	912	103,134
	10 20 30 40 50 60 MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR GLEIEMQRIR 70 80 90 100 110 120 QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE EEVEGEEGGM VVEMDVEWRP 130 140 150 160 170 180 GSRRSAASSA VSSVGARSRG LGGYHGAGHP SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL 190 200 210 220 230 240 EGQPPRVAWA ERLVRGLRGL WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG 250 260 270 280 290 300 MMSSNVYYYT RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 310 320 330 340 350 360 TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV SSEDRAPFGP 370 380 390 400 410 420 RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE ETAAQVASLK KNVWLDRGTR 430 440 450 460 470 480 ATFIDFSVYN ANINLFCVVR LLVEFPATGG VIPSWQFQPL KLIRYVTTFD FFLAACEIIF 490 500 510 520 530 540 CFFIFYYVVE EILEIRIHKL HYFRSFWNCL DVVIVVLFKF INFNRTMSQL STTMSRCAKD 550 560 570 580 590 600 LFGFAIMFFI IFLAYAQLAY LVFGTQVDDF STFQECIFTQ FRIILGDINF AEIEEANRVL 610 620 630 640 650 660 GPIYFTTFVF FMFFILLNMF LAIINDTYSE VKSDLAQQKA EMELSDLIRK GYHKALVKLK 670 680 690 700 710 720 LKKNTVDDIS ESLRQGGGKL NFDELRQDLK GKGHTDAEIE AIFTKYDQDG DQELTEHEHQ 730 740 750 760 770 780 QMRDDLEKER EDLDLDHSSL PRPMSSRSFP RSLDDSEEDD DEDSGHSSRR RGSISSGVSY 790 800 810 820 830 840 EEFQVLVRRV DRMEHSIGSI VSKIDAVIVK LEIMERAKLK RREVLGRLLD GVAEDERLGR 850 860 870 880 890 900 DSEIHREQME RLVREELERW ESDDAASQIS HGLGTPVGLN GQPRPRSSRP SSSQSTEGME 910 GAGGNGSSNV HV
	Isoform 4 (delta9) [UniParc]. Checksum: C3773DAF9FFDB249	FASTA	646	73,171
	10 20 30 40 50 60 MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR GLEIEMQRIR 70 80 90 100 110 120 QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE EEVEGEEGGM VVEMDVEWRP 130 140 150 160 170 180 GSRRSAASSA VSSVGARSRG LGGYHGAGHP SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL 190 200 210 220 230 240 EGQPPRVAWA ERLVRGLRGL WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG 250 260 270 280 290 300 MMSSNVYYYT RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 310 320 330 340 350 360 TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV SSEDRAPFGP 370 380 390 400 410 420 RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE ETAAQVASLK KNVWLDRGTR 430 440 450 460 470 480 ATFIDFSVYN ANINLFCVVR LLVEFPATGG VIPSWQFQPL KLIRYVTTFD FFLAACEIIF 490 500 510 520 530 540 CFFIFYYVVE EILEIRIHKL HYFRSFWNCL DVVIVVLSVV AIGINIYRTS NVEVLLQFLE 550 560 570 580 590 600 DQNTFPNFEH LAYWQIQFNN IAAVTVFFVW IKLFKFINFN RTMSQLSTTM SRCAKDLFGF 610 620 630 640 AIMFFIIFLA YAQLAYLVFG TQVDDFSTFQ ECIICSWRSS MIRTLK
	Isoform 5 (delta12/13) [UniParc]. Checksum: 887260C960F987BE	FASTA	874	98,838
	10 20 30 40 50 60 MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR GLEIEMQRIR 70 80 90 100 110 120 QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE EEVEGEEGGM VVEMDVEWRP 130 140 150 160 170 180 GSRRSAASSA VSSVGARSRG LGGYHGAGHP SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL 190 200 210 220 230 240 EGQPPRVAWA ERLVRGLRGL WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG 250 260 270 280 290 300 MMSSNVYYYT RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 310 320 330 340 350 360 TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV SSEDRAPFGP 370 380 390 400 410 420 RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE ETAAQVASLK KNVWLDRGTR 430 440 450 460 470 480 ATFIDFSVYN ANINLFCVVR LLVEFPATGG VIPSWQFQPL KLIRYVTTFD FFLAACEIIF 490 500 510 520 530 540 CFFIFYYVVE EILEIRIHKL HYFRSFWNCL DVVIVVLSVV AIGINIYRTS NVEVLLQFLE 550 560 570 580 590 600 DQNTFPNFEH LAYWQIQFNN IAAVTVFFVW IKLFKFINFN RTMSQLSTTM SRCAKDLFGF 610 620 630 640 650 660 AIMFFIIFLA YAQLAYLVFG TQVDDFSTFQ ECIFTQFRII LGDINFAEIE EANRVLGPIY 670 680 690 700 710 720 FTTFVFFMFF ILLNMFLAII NDTYSEVKSD LAQQKAEMEL SDLIRKGYHK ALVKLKLKKN 730 740 750 760 770 780 TVDDISESLR QGGGKLNFDE LRQDLKGLVR RVDRMEHSIG SIVSKIDAVI VKLEIMERAK 790 800 810 820 830 840 LKRREVLGRL LDGVAEDERL GRDSEIHREQ MERLVREELE RWESDDAASQ ISHGLGTPVG 850 860 870 LNGQPRPRSS RPSSSQSTEG MEGAGGNGSS NVHV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein." Mochizuki T., Wu G., Hayashi T., Xenophontos S.L., Veldhuisen B., Saris J.J., Reynolds D.M., Cai Y., Gabow P.A., Pierides A., Kimberling W.J., Breuning M.H., Deltas C.C., Peters D.J.M., Somlo S. Science 272:1339-1342(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]	"Characterization of the exon structure of the polycystic kidney disease 2 gene (PKD2)." Hayashi T., Mochizuki T., Reynolds D.M., Wu G., Cai Y., Somlo S. Genomics 44:131-136(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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), VARIANT PRO-28.
[4]	"A gene similar to PKD1 maps to chromosome 4q22: a candidate gene for PKD2." Schneider M.C., Rodriguez A., Nomura H., Zhou J., Morton C.C., Reeders S.T., Weremowicz S. Genomics 38:1-4(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 361-968 (ISOFORM 1). Tissue: Mammary gland.
[5]	"In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2." Lehtonen S., Ora A., Olkkonen V.M., Geng L., Zerial M., Somlo S., Lehtonen E. J. Biol. Chem. 275:32888-32893(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CD2AP.
[6]	"The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton." Gallagher A.R., Cedzich A., Gretz N., Somlo S., Witzgall R. Proc. Natl. Acad. Sci. U.S.A. 97:4017-4022(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HAX1, SUBCELLULAR LOCATION.
[7]	"Polycystin channels and kidney disease." Stayner C., Zhou J. Trends Pharmacol. Sci. 22:543-546(2001) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[8]	"A splice form of polycystin-2, lacking exon 7, does not interact with polycystin-1." Hackmann K., Markoff A., Qian F., Bogdanova N., Germino G.G., Pennekamp P., Dworniczak B., Horst J., Gerke V. Hum. Mol. Genet. 14:3249-3262(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 2; 3; 4 AND 5).
[9]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-812, MASS SPECTROMETRY.
[10]	"Domain mapping of the polycystin-2 C-terminal tail using de novo molecular modeling and biophysical analysis." Celic A., Petri E.T., Demeler B., Ehrlich B.E., Boggon T.J. J. Biol. Chem. 283:28305-28312(2008) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING, PROTEIN SEQUENCE OF 711-715; 720-724; 804-808 AND 823-827, MASS SPECTROMETRY, DOMAIN, CALCIUM-BINDING, CIRCULAR DICHROISM, SUBUNIT, MUTAGENESIS OF THR-771; GLU-774; LEU-842; VAL-846; MET-849; ILE-853; ILE-856 AND VAL-863.
[11]	"A spectrum of mutations in the second gene for autosomal dominant polycystic kidney disease (PKD2)." Veldhuisen B., Saris J.J., de Haij S., Hayashi T., Reynolds D.M., Mochizuki T., Elles R., Fossdal R., Bogdanova N., van Dijk M.A., Coto E., Ravine D., Noerby S., Verellen-Dumoulin C., Breuning M.H., Somlo S., Peters D.J.M. Am. J. Hum. Genet. 61:547-555(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PKD2 GLY-414.
[12]	"Aberrant splicing in the PKD2 gene as a cause of polycystic kidney disease." Reynolds D.M., Hayashi T., Cai Y., Veldhuisen B., Watnick T.J., Lens X.M., Mochizuki T., Qian F., Maeda Y., Li L., Fossdal R., Coto E., Wu G., Breuning M.H., Germino G.G., Peters D.J.M., Somlo S. J. Am. Soc. Nephrol. 10:2342-2351(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PKD2 VAL-511.
[13]	"Seven novel mutations of the PKD2 gene in families with autosomal dominant polycystic kidney disease." Torra R., Viribay M., Telleria D., Badenas C., Watson M., Harris P.C., Darnell A., San Millan J.L. Kidney Int. 56:28-33(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PKD2 PRO-356, VARIANT PRO-28.
[14]	"Mutations of PKD1 in ADPKD2 cysts suggest a pathogenic effect of trans-heterozygous mutations." Watnick T.J., He N., Wang K., Liang Y., Parfrey P., Hefferton D., St George-Hyslop P.H., Germino G.G., Pei Y. Nat. Genet. 25:143-144(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PKD2 ILE-479 DEL; 504-ARG--VAL-512 DEL AND TYR-684 DEL.
[15]	"Four novel mutations of the PKD2 gene in Czech families with autosomal dominant polycystic kidney disease." Reiterova J., Stekrova J., Peters D.J.M., Kapras J., Kohoutova M., Merta M., Zidovska J. Hum. Mutat. 19:573-573(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PKD2 TRP-322, VARIANTS LEU-24; PRO-28 AND LEU-800.
[16]	"Genotype-renal function correlation in type 2 autosomal dominant polycystic kidney disease." Magistroni R., He N., Wang K., Andrew R., Johnson A., Gabow P., Dicks E., Parfrey P., Torra R., San-Millan J.L., Coto E., Van Dijk M., Breuning M., Peters D., Bogdanova N., Ligabue G., Albertazzi A., Hateboer N. , Demetriou K., Pierides A., Deltas C., St George-Hyslop P., Ravine D., Pei Y. J. Am. Soc. Nephrol. 14:1164-1174(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PKD2 PRO-356; GLY-414; ARG-632 AND GLN-807.
[17]	"PKD2 mutations in a Czech population with autosomal dominant polycystic kidney disease." Stekrova J., Reiterova J., Merta M., Damborsky J., Zidovska J., Kebrdlova V., Kohoutova M. Nephrol. Dial. Transplant. 19:1116-1122(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PKD2 GLN-306 AND GLY-420, VARIANT PRO-28.
[18]	"Genetics and phenotypic characteristics of autosomal dominant polycystic kidney disease in Finns." Peltola P., Lumiaho A., Miettinen R., Pihlajamaeki J., Sandford R., Laakso M. J. Mol. Med. 83:638-646(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PKD2 GLN-322.
[19]	"Novel method for genomic analysis of PKD1 and PKD2 mutations in autosomal dominant polycystic kidney disease." Tan Y.-C., Blumenfeld J.D., Anghel R., Donahue S., Belenkaya R., Balina M., Parker T., Levine D., Leonard D.G.B., Rennert H. Hum. Mutat. 30:264-273(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PRO-28; THR-190 AND CYS-482.
[20]	"Novel PKD1 and PKD2 mutations in autosomal dominant polycystic kidney disease (ADPKD)." Hoefele J., Mayer K., Scholz M., Klein H.G. Nephrol. Dial. Transplant. 26:2181-2188(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PKD2 PRO-384.
+	Additional computationally mapped references.

Web resources

GeneReviews

Functional Glycomics Gateway - Glycan Binding

Polycystin 2 - Not a C-type lectin

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U50928 mRNA. Translation: AAC50520.1.
AF004873 , AF004859, AF004860, AF004861, AF004862, AF004863, AF004864, AF004865, AF004866, AF004867, AF004868, AF004869, AF004870, AF004871, AF004872 Genomic DNA. Translation: AAC16004.1.
BC112261 mRNA. Translation: AAI12262.1.
BC112263 mRNA. Translation: AAI12264.1.
U56813 mRNA. Translation: AAC50933.1.

IPI

IPI00299040.

PIR

G02640.

RefSeq

NP_000288.1. NM_000297.3.

UniGene

Hs.181272.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KLD	NMR	-	A	680-796	[»]
2KLE	NMR	-	A	680-796	[»]
2KQ6	NMR	-	A	720-797	[»]
2Y4Q	NMR	-	A	717-792	[»]
3HRN	X-ray	1.90	A	833-895	[»]
3HRO	X-ray	1.90	A	833-872	[»]

ProteinModelPortal

Q13563.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47455N.

MINT

MINT-6618167.

STRING

9606.ENSP00000237596.

Protein family/group databases

TCDB

1.A.5.2.1. polycystin cation channel (PCC) family.

PTM databases

PhosphoSite

Q13563.

Polymorphism databases

DMDM

116242717.

Proteomic databases

PaxDb

Q13563.

PeptideAtlas

Q13563.

PRIDE

Q13563.

Protocols and materials databases

DNASU

5311.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000237596; ENSP00000237596; ENSG00000118762.

GeneID

5311.

KEGG

hsa:5311.

UCSC

uc003hre.3. human.

Organism-specific databases

CTD

5311.

GeneCards

GC04P088929.

HGNC

HGNC:9009. PKD2.

HPA

CAB004544.
HPA015794.

MIM

173910. gene.
613095. phenotype.

neXtProt

NX_Q13563.

Orphanet

730. Autosomal dominant polycystic kidney disease.

PharmGKB

PA33343.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG325704.

HOGENOM

HOG000230858.

HOVERGEN

HBG014945.

InParanoid

Q13563.

KO

K04986.

OMA

AWSRDNP.

OrthoDB

EOG473PQQ.

PhylomeDB

Q13563.

Gene expression databases

ArrayExpress

Q13563.

Bgee

Q13563.

CleanEx

HS_PKD2.

Genevestigator

Q13563.

GermOnline

ENSG00000118762. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.

InterPro

IPR011992. EF-hand-like_dom.
IPR002048. EF_hand_dom.
IPR013122. PKD1_2_channel.
IPR003915. PKD_2.
[Graphical view]

Pfam

PF08016. PKD_channel. 1 hit.
[Graphical view]

PRINTS

PR01433. POLYCYSTIN2.

PROSITE

PS00018. EF_HAND_1. False negative.
PS50222. EF_HAND_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q13563.

ChEMBL

CHEMBL5465.

ChiTaRS

PKD2. human.

EvolutionaryTrace

Q13563.

GenomeRNAi

5311.

NextBio

20536.

SOURCE

Search...

Entry information

Entry name

PKD2_HUMAN

Accession

Primary (citable) accession number: Q13563
Secondary accession number(s): O60441 , Q15764, Q2M1Q3, Q2M1Q5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 135 of the entry and version 3 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.