Q6IVV8 · PKD2_DANRE
- ProteinPolycystin-2
- Genepkd2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids904 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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. Can also form a functional, homotetrameric ion channel (By similarity).
Functions as non-selective, voltage-gated cation channel (By similarity).
Required for normal oscillation of Ca2+ levels within cilia; these oscillations of the intraciliary Ca2+ levels can trigger cytoplasmic Ca2+ signaling cascades (PubMed:25660539).
May contribute to the release of Ca2+ stores from the endoplasmic reticulum (By similarity).
Required for normal temporal variation of the intracellular Ca2+ levels in the heart (PubMed:23376035).
Plays a role in fluid-flow mechanosensation (By similarity).
Required for normal specification of the body left-right axis during embryogenesis, most likely via its role in ciliary Ca2+ oscillations in Kupffer's vesicle (PubMed:15269167, PubMed:16216239, PubMed:16943304, PubMed:17360770, PubMed:23376035, PubMed:25660539).
Functions as non-selective, voltage-gated cation channel (By similarity).
Required for normal oscillation of Ca2+ levels within cilia; these oscillations of the intraciliary Ca2+ levels can trigger cytoplasmic Ca2+ signaling cascades (PubMed:25660539).
May contribute to the release of Ca2+ stores from the endoplasmic reticulum (By similarity).
Required for normal temporal variation of the intracellular Ca2+ levels in the heart (PubMed:23376035).
Plays a role in fluid-flow mechanosensation (By similarity).
Required for normal specification of the body left-right axis during embryogenesis, most likely via its role in ciliary Ca2+ oscillations in Kupffer's vesicle (PubMed:15269167, PubMed:16216239, PubMed:16943304, PubMed:17360770, PubMed:23376035, PubMed:25660539).
Activity regulation
Channel activity is regulated by phosphorylation. Channel activity is regulated by intracellular Ca2+.
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePolycystin-2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionQ6IVV8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Basolateral cell membrane ; Multi-pass membrane protein
Apical cell membrane ; Multi-pass membrane protein
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Note: Detected at the basolateral cell membrane and on apical, lumenal cilia in anterior, proximal pronephric ducts, and in intracellular vesicles in the posterior part of the pronephric duct. Detected on apical cell membranes on epithelial cells in the ear.
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-155 | Cytoplasmic | ||||
Sequence: MSSSRVRPQAPQSPAASASASPPPHEGIEMEKMHHEEVGLGVPDETPSSPPTSSSRQAWSRDNPGFEPEEGMMEADWPPESQGRRSVSTTSSSSSGGVPGNFSGISARINRGLYPTPPAQEHRSCGKRILEKMRVLWDTRLLGESNSNREMYLKT | ||||||
Transmembrane | 156-177 | Helical; Name=S1 | ||||
Sequence: VLREMITYILFLLTLCIITYGM | ||||||
Topological domain | 178-404 | Extracellular | ||||
Sequence: VSTNMYYYTKVMSQLFLDTPLSSGEPTNFKSLSTMEDFWKFTEGPFLNGMYWELWYNNKSLPENQSLIYYENLLLGVPRLRQLRVRNESCSVHEDLRDEVYDCYNVYSPANEDKAPFGPKNGTAWRFKDESSLGESSYWGQVSTYGGGGYYQDLSRTREKSANQLQELKNNLWLDRGTRAVFLDFSIYNGNVNLFCIVRLLVEFPATGGAVPSWQFQTVRLLRYVSS | ||||||
Transmembrane | 405-425 | Helical; Name=S2 | ||||
Sequence: WDYFVGMCEVSFCLFVLYYLV | ||||||
Topological domain | 426-441 | Cytoplasmic | ||||
Sequence: EEALEIRLHRLRYFKS | ||||||
Transmembrane | 442-462 | Helical; Name=S3 | ||||
Sequence: LWNCLDVLIVALSVPAIIMNI | ||||||
Topological domain | 463-489 | Extracellular | ||||
Sequence: CRTSAVSHRLHFLLENHSTYPNFEPLA | ||||||
Transmembrane | 490-510 | Helical; Name=S4 | ||||
Sequence: RLQVHFNNLAAIIVFLSWVKL | ||||||
Topological domain | 511-534 | Cytoplasmic | ||||
Sequence: FKFINFNKTMNQLSTTMSRCAKDL | ||||||
Transmembrane | 535-556 | Helical; Name=5 | ||||
Sequence: MGFAIMFFIVFLAYAQLAYLVF | ||||||
Topological domain | 557-568 | Extracellular | ||||
Sequence: GTQVNDFSTFQA | ||||||
Intramembrane | 569-583 | Pore-forming | ||||
Sequence: CIFTQFRIILGDFDF | ||||||
Topological domain | 584-591 | Extracellular | ||||
Sequence: SEIEEADS | ||||||
Transmembrane | 592-612 | Helical; Name=S6 | ||||
Sequence: VLGPIYFTTFVFFIFMILLNM | ||||||
Topological domain | 613-904 | Cytoplasmic | ||||
Sequence: FLAIINDTYSEVKADMAQQRSEMEITDLIKKSYNRAMVKLKLKKSSINDIPDSLQQAAGKLSFDELRQDLRGKGHSDAEIEAIFAKYDLDGDQELTEHEHQQMRDDLEKEREDLDLEHSSLPRPASGRSFSRSQDDSEEDDDEDSGHSSRRRGSSSGGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEAMERAKMKRRDVLGRILDGVMEDERMGRDPELQREQMDRLVRDELERWESDDTMSQVSHHHHQATPIISSAQLRPRSSRPPSSLSNEGPDAAASGPAHL |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Morpholino knockdown of the protein impairs specification of the left-right axis during embryonic development and randomization of heart and gut looping, plus misexpression of left-side specific genes (PubMed:16216239, PubMed:16943304, PubMed:17360770, PubMed:25660539, PubMed:26432887).
Morpholino knockdown of the protein causes body curvature, tail curling, hydrocephalus and kidney cysts (PubMed:15269167, PubMed:16216239, PubMed:16551655, PubMed:16943304, PubMed:17360770, PubMed:23376035, PubMed:26432887).
Morpholino knockdown has no effect on number, length or motility of pronephric cilia, but the fluid flow through the pronephric ducts seems to be impaired due to physical obstruction of the ducts (PubMed:16943304).
Likewise, morpholino knockdown of the protein has no effect on the motility of cilia in Kupffer's vesicle (PubMed:25660539).
Morpholino knockdown of the protein leads to an increase of the volume of Kupffer's vesicle, without any change in the proliferation of the cells that line the vesicle (PubMed:26432887).
Morpholino knockdown of the protein leads to impaired heart function, characterized by arrhytmia and frequently associated with pericardial and abdominal edema and atrioventricular block (PubMed:23376035).
Morpholino knockdown of the protein causes body curvature, tail curling, hydrocephalus and kidney cysts (PubMed:15269167, PubMed:16216239, PubMed:16551655, PubMed:16943304, PubMed:17360770, PubMed:23376035, PubMed:26432887).
Morpholino knockdown has no effect on number, length or motility of pronephric cilia, but the fluid flow through the pronephric ducts seems to be impaired due to physical obstruction of the ducts (PubMed:16943304).
Likewise, morpholino knockdown of the protein has no effect on the motility of cilia in Kupffer's vesicle (PubMed:25660539).
Morpholino knockdown of the protein leads to an increase of the volume of Kupffer's vesicle, without any change in the proliferation of the cells that line the vesicle (PubMed:26432887).
Morpholino knockdown of the protein leads to impaired heart function, characterized by arrhytmia and frequently associated with pericardial and abdominal edema and atrioventricular block (PubMed:23376035).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 351 | In ty30b; curly tail phenotype and impaired left-right patterning. | ||||
Sequence: L → P |
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000439854 | 1-904 | Polycystin-2 | |||
Sequence: MSSSRVRPQAPQSPAASASASPPPHEGIEMEKMHHEEVGLGVPDETPSSPPTSSSRQAWSRDNPGFEPEEGMMEADWPPESQGRRSVSTTSSSSSGGVPGNFSGISARINRGLYPTPPAQEHRSCGKRILEKMRVLWDTRLLGESNSNREMYLKTVLREMITYILFLLTLCIITYGMVSTNMYYYTKVMSQLFLDTPLSSGEPTNFKSLSTMEDFWKFTEGPFLNGMYWELWYNNKSLPENQSLIYYENLLLGVPRLRQLRVRNESCSVHEDLRDEVYDCYNVYSPANEDKAPFGPKNGTAWRFKDESSLGESSYWGQVSTYGGGGYYQDLSRTREKSANQLQELKNNLWLDRGTRAVFLDFSIYNGNVNLFCIVRLLVEFPATGGAVPSWQFQTVRLLRYVSSWDYFVGMCEVSFCLFVLYYLVEEALEIRLHRLRYFKSLWNCLDVLIVALSVPAIIMNICRTSAVSHRLHFLLENHSTYPNFEPLARLQVHFNNLAAIIVFLSWVKLFKFINFNKTMNQLSTTMSRCAKDLMGFAIMFFIVFLAYAQLAYLVFGTQVNDFSTFQACIFTQFRIILGDFDFSEIEEADSVLGPIYFTTFVFFIFMILLNMFLAIINDTYSEVKADMAQQRSEMEITDLIKKSYNRAMVKLKLKKSSINDIPDSLQQAAGKLSFDELRQDLRGKGHSDAEIEAIFAKYDLDGDQELTEHEHQQMRDDLEKEREDLDLEHSSLPRPASGRSFSRSQDDSEEDDDEDSGHSSRRRGSSSGGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEAMERAKMKRRDVLGRILDGVMEDERMGRDPELQREQMDRLVRDELERWESDDTMSQVSHHHHQATPIISSAQLRPRSSRPPSSLSNEGPDAAASGPAHL | ||||||
Glycosylation | 235 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 241 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 264 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 267↔280 | |||||
Sequence: CSVHEDLRDEVYDC | ||||||
Glycosylation | 298 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 478 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Phosphorylated. Phosphorylation is important for protein function; a mutant human construct that lacks the N-terminal phosphorylation sites cannot complement a zebrafish pkd2-deficient mutant.
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected along cilia and at the cilium basal body in Kupffer's vesicle at the 10 somite stage (PubMed:26432887).
Detected in heart at 48hpf (PubMed:23376035).
Detected in muscle and pronephric kidney at 48 hpf (PubMed:16943304).
Detected on trunk muscle sarcolemma and sarcomere, on ependymal cell cilia in brain, at the apical cell membrane in epithelial cells in the ear, at the lateral line organ and olfactory placode at 56 hpf (PubMed:16943304).
Detected in adult kidney (at protein level) (PubMed:16943304).
Detected in heart at 48hpf (PubMed:23376035).
Detected in muscle and pronephric kidney at 48 hpf (PubMed:16943304).
Detected on trunk muscle sarcolemma and sarcomere, on ependymal cell cilia in brain, at the apical cell membrane in epithelial cells in the ear, at the lateral line organ and olfactory placode at 56 hpf (PubMed:16943304).
Detected in adult kidney (at protein level) (PubMed:16943304).
Developmental stage
First detected at the onset of gastrulation in a band at the blastoderm margin (PubMed:16216239, PubMed:17360770).
Ubiquitous during gastrulation, somatogenesis and at 48 hpf (PubMed:16943304).
During gastrulation, detected at the hypoblast of the dorsal midline and in dorsal forerunner cells that form a ciliated Kupffer's vesicle later on (PubMed:16216239, PubMed:17360770, PubMed:26432887).
Ubiquitous during early somite stages, with high levels of expression in Kupffer's vesicle (PubMed:16216239, PubMed:17360770).
At subsequent stages, detected in pronephric duct primordia and neural floorplate (PubMed:16216239, PubMed:16943304, PubMed:17360770, PubMed:26432887).
Highly expressed in brain at 24 hpf (PubMed:16216239).
At 3 dpf, detected at pharyngeal arches and the pectoral fin bud (PubMed:16216239).
Ubiquitous during gastrulation, somatogenesis and at 48 hpf (PubMed:16943304).
During gastrulation, detected at the hypoblast of the dorsal midline and in dorsal forerunner cells that form a ciliated Kupffer's vesicle later on (PubMed:16216239, PubMed:17360770, PubMed:26432887).
Ubiquitous during early somite stages, with high levels of expression in Kupffer's vesicle (PubMed:16216239, PubMed:17360770).
At subsequent stages, detected in pronephric duct primordia and neural floorplate (PubMed:16216239, PubMed:16943304, PubMed:17360770, PubMed:26432887).
Highly expressed in brain at 24 hpf (PubMed:16216239).
At 3 dpf, detected at pharyngeal arches and the pectoral fin bud (PubMed:16216239).
Gene expression databases
Interaction
Subunit
Component of the heterotetrameric polycystin channel complex with pkd1; the tetramer contains one pkd1 chain and three pkd2 chains (By similarity).
Homotetramer (By similarity).
Interacts with pkd1l1 (By similarity).
Homotetramer (By similarity).
Interacts with pkd1l1 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Polar residues | ||||
Sequence: MSSSRVRPQAPQSPAA | ||||||
Region | 1-102 | Disordered | ||||
Sequence: MSSSRVRPQAPQSPAASASASPPPHEGIEMEKMHHEEVGLGVPDETPSSPPTSSSRQAWSRDNPGFEPEEGMMEADWPPESQGRRSVSTTSSSSSGGVPGNF | ||||||
Compositional bias | 27-41 | Basic and acidic residues | ||||
Sequence: GIEMEKMHHEEVGLG | ||||||
Compositional bias | 46-61 | Polar residues | ||||
Sequence: TPSSPPTSSSRQAWSR | ||||||
Compositional bias | 82-101 | Polar residues | ||||
Sequence: QGRRSVSTTSSSSSGGVPGN | ||||||
Motif | 578-580 | Selectivity filter | ||||
Sequence: LGD | ||||||
Domain | 687-722 | EF-hand 1 | ||||
Sequence: HSDAEIEAIFAKYDLDGDQELTEHEHQQMRDDLEKE | ||||||
Compositional bias | 708-731 | Basic and acidic residues | ||||
Sequence: TEHEHQQMRDDLEKEREDLDLEHS | ||||||
Region | 708-770 | Disordered | ||||
Sequence: TEHEHQQMRDDLEKEREDLDLEHSSLPRPASGRSFSRSQDDSEEDDDEDSGHSSRRRGSSSGG | ||||||
Region | 740-759 | Linker | ||||
Sequence: RSFSRSQDDSEEDDDEDSGH | ||||||
Domain | 768-786 | EF-hand 2 | ||||
Sequence: SGGVSYEEFQVLVRRVDRM | ||||||
Coiled coil | 770-809 | |||||
Sequence: GVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEAMER | ||||||
Region | 854-904 | Disordered | ||||
Sequence: ESDDTMSQVSHHHHQATPIISSAQLRPRSSRPPSSLSNEGPDAAASGPAHL | ||||||
Compositional bias | 864-894 | Polar residues | ||||
Sequence: HHHHQATPIISSAQLRPRSSRPPSSLSNEGP |
Domain
The C-terminal coiled-coil domain is involved in oligomerization. The coiled-coil domain binds calcium and undergoes a calcium-induced conformation change (in vitro).
Sequence similarities
Belongs to the polycystin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length904
- Mass (Da)103,269
- Last updated2004-07-05 v1
- Checksum53B45F174BB50E5E
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8M6YVJ7 | A0A8M6YVJ7_DANRE | pkd2 | 903 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Polar residues | ||||
Sequence: MSSSRVRPQAPQSPAA | ||||||
Sequence conflict | 15 | in Ref. 2; ABA60692 | ||||
Sequence: A → V | ||||||
Compositional bias | 27-41 | Basic and acidic residues | ||||
Sequence: GIEMEKMHHEEVGLG | ||||||
Compositional bias | 46-61 | Polar residues | ||||
Sequence: TPSSPPTSSSRQAWSR | ||||||
Compositional bias | 82-101 | Polar residues | ||||
Sequence: QGRRSVSTTSSSSSGGVPGN | ||||||
Sequence conflict | 130 | in Ref. 2; ABA60692 | ||||
Sequence: L → P | ||||||
Sequence conflict | 325 | in Ref. 2; ABA60692 | ||||
Sequence: G → R | ||||||
Sequence conflict | 334 | in Ref. 2; ABA60692 | ||||
Sequence: T → A | ||||||
Sequence conflict | 604-608 | in Ref. 2; ABA60692 | ||||
Sequence: FIFMI → LIFMV | ||||||
Compositional bias | 708-731 | Basic and acidic residues | ||||
Sequence: TEHEHQQMRDDLEKEREDLDLEHS | ||||||
Compositional bias | 864-894 | Polar residues | ||||
Sequence: HHHHQATPIISSAQLRPRSSRPPSSLSNEGP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY618926 EMBL· GenBank· DDBJ | AAT39122.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ175629 EMBL· GenBank· DDBJ | ABA60692.1 EMBL· GenBank· DDBJ | mRNA | ||
CR788312 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |