Protein

Polycystin-2

Gene

PKD2

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B (PubMed:27214281). Can also form a functional, homotetrameric ion channel (PubMed:29899465). Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:18695040). Functions as outward-rectifying K⁺ channel, but is also permeable to Ca²⁺, and to a much lesser degree also to Na⁺ (PubMed:11854751, PubMed:15692563, PubMed:27071085, PubMed:27991905). May contribute to the release of Ca²⁺ stores from the endoplasmic reticulum (PubMed:11854751, PubMed:20881056). Together with TRPV4, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells. Acts as a regulator of cilium length, together with PKD1. 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. Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning. Detection of asymmetric nodal flow gives rise to a Ca²⁺ signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality (By similarity).By similarityCurated8 Publications

Miscellaneous

The mechanisms that govern channel opening are complex and still under debate; heterologous expression of PKD2 by itself or together with PKD1 gives rise to very low or undetectable spontaneous ion channel activity, in spite of its presence at the cell membrane.2 Publications

Activity regulationⁱ

Channel activity is regulated by phosphorylation (PubMed:16551655, PubMed:20881056, PubMed:26269590). Channel activity is regulated by intracellular Ca²⁺ (PubMed:11854751).4 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	763	CalciumCombined sources1 Publication	1
Metal bindingⁱ	765	CalciumCombined sources1 Publication	1
Metal bindingⁱ	767	CalciumCombined sources1 Publication	1
Metal bindingⁱ	769	Calcium; via carbonyl oxygenCombined sources1 Publication	1
Metal bindingⁱ	774	CalciumCombined sources1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Calcium bindingⁱ	763 – 774	PROSITE-ProRule annotationCombined sources2 PublicationsAdd BLAST		12

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Calcium channel, Ion channel, Potassium channel, Voltage-gated channel
Biological process	Calcium transport, Ion transport, Potassium transport, Transport, Wnt signaling pathway
Ligand	Calcium, Metal-binding, Potassium

Enzyme and pathway databases

PathwayCommonsⁱ	Q13563
Reactomeⁱ	R-HSA-5620916, VxPx cargo-targeting to cilium
SIGNORⁱ	Q13563

Protein family/group databases

TCDBⁱ	1.A.5.2.1, the polycystin cation channel (pcc) family

TCDBⁱ

1.A.5.2.1, the polycystin cation channel (pcc) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Polycystin-2Curated Short name: PC21 Publication Alternative name(s): Autosomal dominant polycystic kidney disease type II protein Polycystic kidney disease 2 protein Polycystwin1 Publication R48321 Transient receptor potential cation channel subfamily P member 21 PublicationImported
Gene namesⁱ	Name:PKD2Imported Synonyms:TRPP21 PublicationImported
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	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
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 4

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9009, PKD2
MIMⁱ	173910, gene
neXtProtⁱ	NX_Q13563
VEuPathDBⁱ	HostDB:ENSG00000118762.7

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 219	Cytoplasmic3 PublicationsAdd BLAST	219
Transmembraneⁱ	220 – 241	Helical; Name=S13 PublicationsAdd BLAST	22
Topological domainⁱ	242 – 468	Extracellular3 PublicationsAdd BLAST	227
Transmembraneⁱ	469 – 489	Helical; Name=S23 PublicationsAdd BLAST	21
Topological domainⁱ	490 – 505	Cytoplasmic3 PublicationsAdd BLAST	16
Transmembraneⁱ	506 – 526	Helical; Name=S33 PublicationsAdd BLAST	21
Topological domainⁱ	527 – 552	Extracellular3 PublicationsAdd BLAST	26
Transmembraneⁱ	553 – 573	Helical; Name=S43 PublicationsAdd BLAST	21
Topological domainⁱ	574 – 597	Cytoplasmic3 PublicationsAdd BLAST	24
Transmembraneⁱ	598 – 619	Helical; Name=53 PublicationsAdd BLAST	22
Topological domainⁱ	620 – 631	Extracellular3 PublicationsAdd BLAST	12
Intramembraneⁱ	632 – 646	Pore-forming3 PublicationsAdd BLAST	15
Topological domainⁱ	647 – 654	Extracellular3 Publications	8
Transmembraneⁱ	655 – 675	Helical; Name=S63 PublicationsAdd BLAST	21
Topological domainⁱ	676 – 968	Cytoplasmic3 PublicationsAdd BLAST	293

Keywords - Cellular componentⁱ

Cell membrane, Cell projection, Cilium, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Polycystic kidney disease 2 with or without polycystic liver disease (PKD2)13 Publications

The disease is caused by variants affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant 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.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_058822	306	R → Q in PKD2. 1 PublicationCorresponds to variant dbSNP:rs990932947Ensembl.	1
Natural variantⁱVAR_058823	322	R → Q in PKD2. 1 PublicationCorresponds to variant dbSNP:rs145877597EnsemblClinVar.	1
Natural variantⁱVAR_058824	322	R → W in PKD2. 1 PublicationCorresponds to variant dbSNP:rs1553925453EnsemblClinVar.	1
Natural variantⁱVAR_011073	356	A → P in PKD2. 2 Publications	1
Natural variantⁱVAR_064394	384	A → P in PKD2. 1 Publication	1
Natural variantⁱVAR_009195	414	W → G in PKD2; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604. 3 Publications	1
Natural variantⁱVAR_058825	420	R → G in PKD2; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604. 2 Publications	1
Natural variantⁱVAR_011074	479	Missing in PKD2; somatic mutation. 1 Publication	1
Natural variantⁱVAR_011075	504 – 512	Missing in PKD2; somatic mutation. 1 Publication	9
Natural variantⁱVAR_058827	511	D → V in PKD2; loss of function in the release of Ca(2+) stores from the endoplasmic reticulum; no effect on location at the endoplasmic reticulum; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604. 5 PublicationsCorresponds to variant dbSNP:rs121918043EnsemblClinVar.	1
Natural variantⁱVAR_058828	632	C → R in PKD2. 1 Publication	1
Natural variantⁱVAR_011076	684	Missing in PKD2; somatic mutation; abolishes channel currents induced by the gain-of-function artificial mutant P-604. 1 Publication	1
Natural variantⁱVAR_058830	807	R → Q in PKD2. 1 PublicationCorresponds to variant dbSNP:rs147654263EnsemblClinVar.	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	76	S → A: Abolishes phosphorylation of the N-terminal domain. Abolishes the ability to complement a pkd2-deficient zebrafish mutant; when associated with A-80. 1 Publication	1
Mutagenesisⁱ	80	S → A: Decreases phosphorylation of the N-terminal domain. Abolishes the ability to complement a pkd2-deficient zebrafish mutant; when associated with A-76. 1 Publication	1
Mutagenesisⁱ	201	W → A: Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication	1
Mutagenesisⁱ	604	F → A or I: No effect on channel activation. 1 Publication	1
Mutagenesisⁱ	604	F → P: Gain-of-function mutation resulting in increased channel activity. Absence of gain of function; when associated with F-605 DEL; when associated with A-201; when associated with V-511; when associated with G-414; when associated with G-420; when associated with Y-684 DEL; when associated with A-684. Increased channel activity; when associated with 736-L-N-737 DEL. 2 Publications	1
Mutagenesisⁱ	605	Missing : Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication	1
Mutagenesisⁱ	677	L → N: Gain of function mutation. 1 Publication	1
Mutagenesisⁱ	684	Y → A: Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication	1
Mutagenesisⁱ	688	K → A: Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication	1
Mutagenesisⁱ	721	T → A: Decreases phosphorylation; when associated with A-801; A-812; A-831 and A-943. 1 Publication	1
Mutagenesisⁱ	736 – 737	Missing : Increased channel activity; when associated with P-604. 1 Publication	2
Mutagenesisⁱ	768	Q → G: Strongly increases calcium binding affinity. 1 Publication	1
Mutagenesisⁱ	771	T → A: Loss of calcium-binding site; when associated with A-774. 1 Publication	1
Mutagenesisⁱ	774	E → A: Loss of calcium-binding site; when associated with A-771. 1 Publication	1
Mutagenesisⁱ	774	E → Q: Abolishes calcium binding via the EF-hand. 1 Publication	1
Mutagenesisⁱ	801	S → A: Decreases phosphorylation; when associated with A-721; A-812; A-831 and A-943. 1 Publication	1
Mutagenesisⁱ	801	S → D: Phosphomimetic mutant. No effect on release of Ca(2+) stores from the endoplasmic reticulum. 1 Publication	1
Mutagenesisⁱ	801	S → G: Loss of phosphorylation at this site. Impairs release of Ca(2+) stores from the endoplasmic reticulum. 1 Publication	1
Mutagenesisⁱ	804	S → N: Loss of phosphorylation at Ser-801. 1 Publication	1
Mutagenesisⁱ	812	S → A: Decreases interaction with PACS1 and enhances expression at the cell membrane. Decreases phosphorylation; when associated with A-721; A-801; A-831 and A-943. 2 Publications	1
Mutagenesisⁱ	812	S → D: No effect on interaction with PACS1. 1 Publication	1
Mutagenesisⁱ	815 – 817	DDD → AAA: Strongly decreases interaction with PACS1 and enhances expression at the cell membrane. 1 Publication	3
Mutagenesisⁱ	829	S → A: Abolishes increased channel opening in response to cAMP and phosphorylation by PKA. 1 Publication	1
Mutagenesisⁱ	831	S → A: Decreases phosphorylation; when associated with A-721; A-801; A-812 and A-943. 1 Publication	1
Mutagenesisⁱ	842	L → A: Abolishes oligomerization and interaction with PKD1; when associated with A-846; A-849; A-860; A-863 and A-867. 1 Publication	1
Mutagenesisⁱ	842	L → P: Loss of protein solubility. 1 Publication	1
Mutagenesisⁱ	846	V → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-849; A-860; A-863 and A-867. 1 Publication	1
Mutagenesisⁱ	846	V → E: Loss of protein solubility. 1 Publication	1
Mutagenesisⁱ	849	M → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-860; A-863 and A-867. 1 Publication	1
Mutagenesisⁱ	849	M → K: Loss of protein solubility. 1 Publication	1
Mutagenesisⁱ	853	I → P: Loss of protein solubility. 1 Publication	1
Mutagenesisⁱ	856	I → K: Loss of protein solubility. 1 Publication	1
Mutagenesisⁱ	860	I → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-863 and A-867. 1 Publication	1
Mutagenesisⁱ	863	V → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-860 and A-867. 1 Publication	1
Mutagenesisⁱ	863	V → E: Loss of protein solubility; when associated with K-849. 1 Publication	1
Mutagenesisⁱ	867	L → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-860 and A-863. 1 Publication	1
Mutagenesisⁱ	943	S → A: Decreases phosphorylation; when associated with A-721; A-801; A-812 and A-831. 1 Publication	1

Keywords - Diseaseⁱ

Ciliopathy, Disease variant

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5311
GeneReviewsⁱ	PKD2
MalaCards human disease database More...MalaCardsⁱ	PKD2
MIMⁱ	613095, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000118762
Orphanetⁱ	730, Autosomal dominant polycystic kidney disease
PharmGKBⁱ	PA33343

Miscellaneous databases

Pharosⁱ	Q13563, Tchem

Pharosⁱ

Q13563, Tchem

Chemistry databases

ChEMBLⁱ	CHEMBL5465
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	504

Genetic variation databases

BioMutaⁱ	PKD2
DMDMⁱ	116242717

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000164356	1 – 968	Polycystin-2Add BLAST		968

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	76	Phosphoserine1 Publication	1
Modified residueⁱ	80	Phosphoserine1 Publication	1
Modified residueⁱ	137	Omega-N-methylarginineBy similarity	1
Glycosylationⁱ	299	N-linked (GlcNAc...) asparagine1 Publication	1
Glycosylationⁱ	305	N-linked (GlcNAc...) asparagine1 Publication	1
Glycosylationⁱ	328	N-linked (GlcNAc...) (complex) asparagine4 Publications	1
Disulfide bondⁱ	331 ↔ 344	Combined sources2 Publications
Glycosylationⁱ	362	N-linked (GlcNAc...) asparagine3 Publications	1
Glycosylationⁱ	375	N-linked (GlcNAc...) asparagine3 Publications	1
Modified residueⁱ	801	Phosphoserine1 Publication1 Publication	1
Modified residueⁱ	808	PhosphoserineBy similarity	1
Modified residueⁱ	812	PhosphoserineCombined sources2 Publications	1
Modified residueⁱ	829	Phosphoserine1 Publication	1

Post-translational modificationⁱ

Phosphorylated. Phosphorylation is important for protein function; a mutant that lacks the N-terminal phosphorylation sites cannot complement a zebrafish pkd2-deficient mutant (PubMed:16551655). PKD-mediated phosphorylation at the C-terminus regulates its function in the release of Ca²⁺ stores from the endoplasmic reticulum (PubMed:20881056). PKA-mediated phosphorylation at a C-terminal site strongly increases the open probability of the channel, but does not increase single channel conductance (PubMed:26269590).3 Publications

N-glycosylated. The four subunits in a tetramer probably differ in the extent of glycosylation; simultaneous glycosylation of all experimentally validated sites would probably create steric hindrance. Thus, glycosylation at Asn-305 is not compatible with glycosylation at Asn-328; only one of these two residues is glycosylated at a given time.1 Publication

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

jPOSTⁱ	Q13563
MassIVEⁱ	Q13563
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q13563
PaxDbⁱ	Q13563
PeptideAtlas More...PeptideAtlasⁱ	Q13563
PRIDEⁱ	Q13563
ProteomicsDBⁱ	59562 [Q13563-1] 59563 [Q13563-2] 59564 [Q13563-3] 59565 [Q13563-4] 59566 [Q13563-5]

PTM databases

GlyGenⁱ	Q13563, 5 sites
iPTMnetⁱ	Q13563
PhosphoSitePlusⁱ	Q13563

Expressionⁱ

Tissue specificityⁱ

Detected in fetal and adult kidney (PubMed:10770959). Detected at the thick ascending limb of the loop of Henle, at distal tubules, including the distal convoluted tubule and cortical collecting tubules, with weak staining of the collecting duct (PubMed:10770959). Detected on placenta syncytiotrophoblasts (at protein level) (PubMed:26269590). Strongly expressed in ovary, fetal and adult kidney, testis, and small intestine. Not detected in peripheral leukocytes.3 Publications

Gene expression databases

Bgeeⁱ	ENSG00000118762, Expressed in thoracic aorta and 244 other tissues
ExpressionAtlasⁱ	Q13563, baseline and differential
Genevisibleⁱ	Q13563, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000118762, Low tissue specificity

HPAⁱ

ENSG00000118762, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

Homotetramer (PubMed:20881056, PubMed:27768895, PubMed:27991905, PubMed:28092368, PubMed:29899465). Heterotetramer with PKD1, giving rise to a complex formed by one PKD1 chain and three PKD2 chains (PubMed:20881056, PubMed:19556541, PubMed:27214281, PubMed:30093605). Interaction with PKD1 is required for ciliary localization (By similarity)

Isoform 1 interacts with PKD1 while isoform 3 does not (By similarity).

Interacts with PKD1L1.

Interacts with CD2AP (PubMed:10913159).

Interacts with HAX1 (PubMed:10760273).

Interacts with NEK8 (By similarity).

Part of a complex containing AKAP5, ADCY5, ADCY6 and PDE4C (By similarity).

Interacts (via C-terminus) with TRPV4 (via C-terminus) (PubMed:18695040).

Interacts (via C-terminal acidic region) with PACS1 and PACS2; these interactions retain the protein in the endoplasmic reticulum and prevent trafficking to the cell membrane (PubMed:15692563).

By similarity9 Publications

Binary interactionsⁱ

Hide details

Q13563

With	#Exp.	IntAct
CYSRT1 [A8MQ03]	3	EBI-7813714,EBI-3867333
HSF2BP [O75031]	3	EBI-7813714,EBI-7116203
ID2 [Q02363]	7	EBI-7813714,EBI-713450
KRT40 [Q6A162]	3	EBI-7813714,EBI-10171697
KRTAP10-8 [P60410]	3	EBI-7813714,EBI-10171774
KRTAP6-2 [Q3LI66]	3	EBI-7813714,EBI-11962084
MAGEA8 [P43361]	4	EBI-7813714,EBI-10182930
MDFI [Q99750]	3	EBI-7813714,EBI-724076
PKD1 [P98161]	8	EBI-7813714,EBI-1752013
PKD1 - isoform 1 [P98161-1]	4	EBI-7813714,EBI-1951183
itself	9	EBI-7813714,EBI-7813714
PLSCR1 [O15162]	3	EBI-7813714,EBI-740019
TRPC1 [P48995]	12	EBI-7813714,EBI-929665
TRPC1 - isoform Short [P48995-2]	4	EBI-7813714,EBI-9830970
Hax1 [O35387] from Mus musculus.	3	EBI-7813714,EBI-642449
itpr1.S [Q91908] from Xenopus laevis.	2	EBI-7813714,EBI-9633447
Trpv4 [Q9EPK8] from Mus musculus.	11	EBI-7813714,EBI-7091763

PKD2 - isoform 1 [Q13563-1]

With	#Exp.	IntAct
PKD1 [P98161]	5	EBI-9837017,EBI-1752013
PKD1 - isoform 3 [P98161-3]	4	EBI-9837017,EBI-15930070
itself	12	EBI-9837017,EBI-9837017
Pkd1 [O08852] from Mus musculus.	2	EBI-9837017,EBI-6666305

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	111328, 62 interactors
ComplexPortalⁱ	CPX-4001, PKD1-PKD2 Polycystin complex
CORUMⁱ	Q13563
Database of interacting proteins More...DIPⁱ	DIP-47455N
ELMⁱ	Q13563
IntActⁱ	Q13563, 41 interactors
Molecular INTeraction database More...MINTⁱ	Q13563
STRINGⁱ	9606.ENSP00000237596

Chemistry databases

BindingDBⁱ	Q13563

BindingDBⁱ

Q13563

Miscellaneous databases

RNActⁱ	Q13563, protein

RNActⁱ

Q13563, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	214 – 241	Combined sources	28
Helixⁱ	247 – 257	Combined sources	11
Helixⁱ	270 – 272	Combined sources	3
Helixⁱ	276 – 284	Combined sources	9
Helixⁱ	286 – 291	Combined sources	6
Beta strandⁱ	304 – 306	Combined sources	3
Turnⁱ	310 – 312	Combined sources	3
Beta strandⁱ	313 – 315	Combined sources	3
Beta strandⁱ	320 – 326	Combined sources	7
Helixⁱ	328 – 330	Combined sources	3
Helixⁱ	335 – 337	Combined sources	3
Turnⁱ	338 – 340	Combined sources	3
Turnⁱ	350 – 352	Combined sources	3
Beta strandⁱ	363 – 367	Combined sources	5
Turnⁱ	371 – 375	Combined sources	5
Beta strandⁱ	382 – 386	Combined sources	5
Beta strandⁱ	390 – 394	Combined sources	5
Helixⁱ	399 – 411	Combined sources	13
Beta strandⁱ	419 – 430	Combined sources	12
Turnⁱ	431 – 434	Combined sources	4
Beta strandⁱ	435 – 444	Combined sources	10
Beta strandⁱ	452 – 460	Combined sources	9
Helixⁱ	468 – 495	Combined sources	28
Turnⁱ	500 – 503	Combined sources	4
Beta strandⁱ	504 – 506	Combined sources	3
Helixⁱ	507 – 527	Combined sources	21
Turnⁱ	528 – 530	Combined sources	3
Helixⁱ	533 – 538	Combined sources	6
Helixⁱ	549 – 572	Combined sources	24
Helixⁱ	573 – 575	Combined sources	3
Helixⁱ	581 – 619	Combined sources	39
Turnⁱ	620 – 622	Combined sources	3
Helixⁱ	624 – 626	Combined sources	3
Helixⁱ	629 – 641	Combined sources	13
Helixⁱ	646 – 652	Combined sources	7
Helixⁱ	656 – 667	Combined sources	12
Helixⁱ	668 – 672	Combined sources	5
Helixⁱ	673 – 697	Combined sources	25
Turnⁱ	730 – 734	Combined sources	5
Helixⁱ	738 – 744	Combined sources	7
Turnⁱ	745 – 747	Combined sources	3
Helixⁱ	752 – 762	Combined sources	11
Beta strandⁱ	763 – 766	Combined sources	4
Beta strandⁱ	767 – 771	Combined sources	5
Helixⁱ	773 – 777	Combined sources	5
Turnⁱ	781 – 783	Combined sources	3
Beta strandⁱ	793 – 795	Combined sources	3
Helixⁱ	836 – 894	Combined sources	59

Show more details

3D structure databases

BMRBⁱ	Q13563
SMRⁱ	Q13563
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q13563

EvolutionaryTraceⁱ

Q13563

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	750 – 785	EF-handPROSITE-ProRule annotation2 PublicationsAdd BLAST		36

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	803 – 822	Linker1 PublicationAdd BLAST		20
Regionⁱ	810 – 821	Important for interaction with PACS1 and PACS21 PublicationAdd BLAST		12

Coiled coil

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Coiled coilⁱ	833 – 872	1 Publication1 PublicationAdd BLAST		40

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	641 – 643	Selectivity filter1 Publication		3

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	95 – 107	Poly-GluAdd BLAST		13
Compositional biasⁱ	153 – 157	Poly-Arg		5

Domainⁱ

The C-terminal coiled-coil domain is involved in oligomerization and the interaction with PKD1 (PubMed:18694932, PubMed:19556541). The isolated coiled-coil domain forms a homotrimer in vitro; the homotrimer interacts with a single PKD1 chain (PubMed:19556541). The coiled-coil domain binds calcium and undergoes a calcium-induced conformation change (in vitro) (PubMed:18694932).2 Publications

Sequence similaritiesⁱ

Belongs to the polycystin family.Curated

Keywords - Domainⁱ

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3599, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000159025
HOGENOMⁱ	CLU_012097_0_0_1
InParanoidⁱ	Q13563
OMAⁱ	YHGAGHP
PhylomeDBⁱ	Q13563
TreeFamⁱ	TF316484

Family and domain databases

Gene3Dⁱ	1.20.120.350, 1 hit
InterProⁱ	View protein in InterPro IPR011992, EF-hand-dom_pair IPR002048, EF_hand_dom IPR013122, PKD1_2_channel IPR003915, PKD_2 IPR027359, Volt_channel_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08016, PKD_channel, 1 hit
PRINTSⁱ	PR01433, POLYCYSTIN2
SUPFAMⁱ	SSF47473, SSF47473, 1 hit
PROSITEⁱ	View protein in PROSITE PS50222, EF_HAND_2, 1 hit

Sequences (5+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 5 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 5 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform 1 (identifier: Q13563-1) [UniParc]FASTA Add to basket

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

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MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR 
        60         70         80         90        100
GLEIEMQRIR QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE 
       110        120        130        140        150
EEVEGEEGGM VVEMDVEWRP GSRRSAASSA VSSVGARSRG LGGYHGAGHP 
       160        170        180        190        200
SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL EGQPPRVAWA ERLVRGLRGL 
       210        220        230        240        250
WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG MMSSNVYYYT 
       260        270        280        290        300
RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 
       310        320        330        340        350
TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV 
       360        370        380        390        400
SSEDRAPFGP RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE 
       410        420        430        440        450
ETAAQVASLK KNVWLDRGTR ATFIDFSVYN ANINLFCVVR LLVEFPATGG 
       460        470        480        490        500
VIPSWQFQPL KLIRYVTTFD FFLAACEIIF CFFIFYYVVE EILEIRIHKL 
       510        520        530        540        550
HYFRSFWNCL DVVIVVLSVV AIGINIYRTS NVEVLLQFLE DQNTFPNFEH 
       560        570        580        590        600
LAYWQIQFNN IAAVTVFFVW IKLFKFINFN RTMSQLSTTM SRCAKDLFGF 
       610        620        630        640        650
AIMFFIIFLA YAQLAYLVFG TQVDDFSTFQ ECIFTQFRII LGDINFAEIE 
       660        670        680        690        700
EANRVLGPIY FTTFVFFMFF ILLNMFLAII NDTYSEVKSD LAQQKAEMEL 
       710        720        730        740        750
SDLIRKGYHK ALVKLKLKKN TVDDISESLR QGGGKLNFDE LRQDLKGKGH 
       760        770        780        790        800
TDAEIEAIFT KYDQDGDQEL TEHEHQQMRD DLEKEREDLD LDHSSLPRPM 
       810        820        830        840        850
SSRSFPRSLD DSEEDDDEDS GHSSRRRGSI SSGVSYEEFQ VLVRRVDRME 
       860        870        880        890        900
HSIGSIVSKI DAVIVKLEIM ERAKLKRREV LGRLLDGVAE DERLGRDSEI 
       910        920        930        940        950
HREQMERLVR EELERWESDD AASQISHGLG TPVGLNGQPR PRSSRPSSSQ 
       960 
STEGMEGAGG NGSSNVHV

Length:968

Mass (Da):109,691

Last modified:October 17, 2006 - v3

Checksum:ⁱF8D2E760EBEA8B47

Isoform 2 (identifier: Q13563-2) [UniParc]FASTA Add to basket

Also known as: delta6

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

« Hide

        10         20         30         40         50
MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR 
        60         70         80         90        100
GLEIEMQRIR QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE 
       110        120        130        140        150
EEVEGEEGGM VVEMDVEWRP GSRRSAASSA VSSVGARSRG LGGYHGAGHP 
       160        170        180        190        200
SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL EGQPPRVAWA ERLVRGLRGL 
       210        220        230        240        250
WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG MMSSNVYYYT 
       260        270        280        290        300
RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 
       310        320        330        340        350
TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV 
       360        370        380        390        400
SSEDRAPFGP RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE 
       410        420        430        440        450
ETAAQVASLK KNVWLDRGTR ATFIDFSVYN ANINLFCVVR LLVEFPATGG 
       460        470        480 
VIPSWQFQPL KLIRYVTTFD FFLAAFICSS YGD

Show »

Length:483

Mass (Da):53,686

Checksum:ⁱ6F4CC2DD18EEF56F

Isoform 3 (identifier: Q13563-3) [UniParc]FASTA Add to basket

Also known as: delta7

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

« Hide

        10         20         30         40         50
MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR 
        60         70         80         90        100
GLEIEMQRIR QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE 
       110        120        130        140        150
EEVEGEEGGM VVEMDVEWRP GSRRSAASSA VSSVGARSRG LGGYHGAGHP 
       160        170        180        190        200
SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL EGQPPRVAWA ERLVRGLRGL 
       210        220        230        240        250
WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG MMSSNVYYYT 
       260        270        280        290        300
RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 
       310        320        330        340        350
TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV 
       360        370        380        390        400
SSEDRAPFGP RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE 
       410        420        430        440        450
ETAAQVASLK KNVWLDRGTR ATFIDFSVYN ANINLFCVVR LLVEFPATGG 
       460        470        480        490        500
VIPSWQFQPL KLIRYVTTFD FFLAACEIIF CFFIFYYVVE EILEIRIHKL 
       510        520        530        540        550
HYFRSFWNCL DVVIVVLFKF INFNRTMSQL STTMSRCAKD LFGFAIMFFI 
       560        570        580        590        600
IFLAYAQLAY LVFGTQVDDF STFQECIFTQ FRIILGDINF AEIEEANRVL 
       610        620        630        640        650
GPIYFTTFVF FMFFILLNMF LAIINDTYSE VKSDLAQQKA EMELSDLIRK 
       660        670        680        690        700
GYHKALVKLK LKKNTVDDIS ESLRQGGGKL NFDELRQDLK GKGHTDAEIE 
       710        720        730        740        750
AIFTKYDQDG DQELTEHEHQ QMRDDLEKER EDLDLDHSSL PRPMSSRSFP 
       760        770        780        790        800
RSLDDSEEDD DEDSGHSSRR RGSISSGVSY EEFQVLVRRV DRMEHSIGSI 
       810        820        830        840        850
VSKIDAVIVK LEIMERAKLK RREVLGRLLD GVAEDERLGR DSEIHREQME 
       860        870        880        890        900
RLVREELERW ESDDAASQIS HGLGTPVGLN GQPRPRSSRP SSSQSTEGME 
       910 
GAGGNGSSNV HV

Show »

Length:912

Mass (Da):103,134

Checksum:ⁱEDD0DB1BD7750772

Isoform 4 (identifier: Q13563-4) [UniParc]FASTA Add to basket

Also known as: delta9

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

« Hide

        10         20         30         40         50
MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR 
        60         70         80         90        100
GLEIEMQRIR QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE 
       110        120        130        140        150
EEVEGEEGGM VVEMDVEWRP GSRRSAASSA VSSVGARSRG LGGYHGAGHP 
       160        170        180        190        200
SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL EGQPPRVAWA ERLVRGLRGL 
       210        220        230        240        250
WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG MMSSNVYYYT 
       260        270        280        290        300
RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 
       310        320        330        340        350
TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV 
       360        370        380        390        400
SSEDRAPFGP RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE 
       410        420        430        440        450
ETAAQVASLK KNVWLDRGTR ATFIDFSVYN ANINLFCVVR LLVEFPATGG 
       460        470        480        490        500
VIPSWQFQPL KLIRYVTTFD FFLAACEIIF CFFIFYYVVE EILEIRIHKL 
       510        520        530        540        550
HYFRSFWNCL DVVIVVLSVV AIGINIYRTS NVEVLLQFLE DQNTFPNFEH 
       560        570        580        590        600
LAYWQIQFNN IAAVTVFFVW IKLFKFINFN RTMSQLSTTM SRCAKDLFGF 
       610        620        630        640 
AIMFFIIFLA YAQLAYLVFG TQVDDFSTFQ ECIICSWRSS MIRTLK

Show »

Length:646

Mass (Da):73,171

Checksum:ⁱC3773DAF9FFDB249

Isoform 5 (identifier: Q13563-5) [UniParc]FASTA Add to basket

Also known as: delta12/13

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

« Hide

        10         20         30         40         50
MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR 
        60         70         80         90        100
GLEIEMQRIR QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE 
       110        120        130        140        150
EEVEGEEGGM VVEMDVEWRP GSRRSAASSA VSSVGARSRG LGGYHGAGHP 
       160        170        180        190        200
SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL EGQPPRVAWA ERLVRGLRGL 
       210        220        230        240        250
WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG MMSSNVYYYT 
       260        270        280        290        300
RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 
       310        320        330        340        350
TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV 
       360        370        380        390        400
SSEDRAPFGP RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE 
       410        420        430        440        450
ETAAQVASLK KNVWLDRGTR ATFIDFSVYN ANINLFCVVR LLVEFPATGG 
       460        470        480        490        500
VIPSWQFQPL KLIRYVTTFD FFLAACEIIF CFFIFYYVVE EILEIRIHKL 
       510        520        530        540        550
HYFRSFWNCL DVVIVVLSVV AIGINIYRTS NVEVLLQFLE DQNTFPNFEH 
       560        570        580        590        600
LAYWQIQFNN IAAVTVFFVW IKLFKFINFN RTMSQLSTTM SRCAKDLFGF 
       610        620        630        640        650
AIMFFIIFLA YAQLAYLVFG TQVDDFSTFQ ECIFTQFRII LGDINFAEIE 
       660        670        680        690        700
EANRVLGPIY FTTFVFFMFF ILLNMFLAII NDTYSEVKSD LAQQKAEMEL 
       710        720        730        740        750
SDLIRKGYHK ALVKLKLKKN TVDDISESLR QGGGKLNFDE LRQDLKGLVR 
       760        770        780        790        800
RVDRMEHSIG SIVSKIDAVI VKLEIMERAK LKRREVLGRL LDGVAEDERL 
       810        820        830        840        850
GRDSEIHREQ MERLVREELE RWESDDAASQ ISHGLGTPVG LNGQPRPRSS 
       860        870 
RPSSSQSTEG MEGAGGNGSS NVHV

Note: Minor isoform.Curated

Show »

Length:874

Mass (Da):98,838

Checksum:ⁱ887260C960F987BE

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	B4DFN3	B4DFN3_HUMAN		Polycystin-2 Polycystin-2 (cDNA FLJ50473, highly similar to Polycystin-2)	PKD2	386	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	45	G → R in AAC16004 (PubMed:9286709).Curated		1
Sequence conflictⁱ	449	G → V in AAC50933 (PubMed:8954772).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_058820	24	P → L1 PublicationCorresponds to variant dbSNP:rs1004860210Ensembl.	1
Natural variantⁱVAR_011072	28	R → P5 PublicationsCorresponds to variant dbSNP:rs1805044EnsemblClinVar.	1
Natural variantⁱVAR_058821	190	A → T1 PublicationCorresponds to variant dbSNP:rs117078377EnsemblClinVar.	1
Natural variantⁱVAR_058822	306	R → Q in PKD2. 1 PublicationCorresponds to variant dbSNP:rs990932947Ensembl.	1
Natural variantⁱVAR_058823	322

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q13563 (PKD2_HUMAN)

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Polycystin-2

PKD2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Golgi apparatus

Endoplasmic reticulum

Plasma membrane

Other locations

Cytoskeleton

Endoplasmic reticulum

Extracellular region or secreted

Golgi apparatus

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Q13563

PKD2 - isoform 1 [Q13563-1]

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Coiled coil

Motif

Compositional bias

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ