E2RK30 · PKHD1_CANLF

Function

function

Promotes ciliogenesis in renal epithelial cells and therefore participates in the tubules formation and/ or ensures the maintenance of the architecture of the lumen of the kidney (By similarity).
Has an impact on cellular symmetry by ensuring correct bipolar cell division through the regulation of centrosome duplication and mitotic spindle assembly and by maintaining oriented cell division (OCD) during tubular elongation through planar cell polarity (PCP) pathway (By similarity).
During epithelial cell morphogenesis regulates also cell-cell and cell-matrix adhesion and participates in cell motility (PubMed:31398719, PubMed:32698519).
Promotes cell-cell contact through the positive regulation of PTK2 kinase activity leading to either positive regulation of epithelial cell proliferation through the HRAS/RAF1 pathways, or negative regulation of apoptosis through the PDK1/AKT1 pathway (By similarity).
May act in collecting-duct and biliary differentiation (By similarity).
May participate in the regulation of the cholangiocytes proliferation and the CCN2 production in an CXCL8-dependent manner (By similarity).

Features

Showing features for site.

140745001,0001,5002,0002,5003,0003,5004,000
TypeIDPosition(s)Description
Site3616-3617Cleavage

GO annotations

AspectTerm
Cellular Componentapical plasma membrane
Cellular Componentchromosome, centromeric region
Cellular Componentcilium
Cellular Componentendoplasmic reticulum
Cellular Componentextracellular exosome
Cellular ComponentGolgi apparatus
Cellular Componentnucleus
Cellular Componentspindle
Biological Processbranching morphogenesis of an epithelial tube
Biological Processcell-cell junction organization
Biological Processepithelial cell morphogenesis
Biological Processestablishment of centrosome localization
Biological Processestablishment of mitotic spindle orientation
Biological Processnegative regulation of epithelial cell apoptotic process
Biological Processpositive regulation of epithelial cell proliferation
Biological Processregulation of cell adhesion
Biological Processregulation of cell-cell adhesion
Biological Processregulation of cell-matrix adhesion
Biological Processregulation of cholangiocyte proliferation
Biological Processregulation of establishment of planar polarity

Names & Taxonomy

Protein names

  • Recommended name
    Fibrocystin
  • Alternative names
    • Polycystic kidney and hepatic disease 1 protein
    • Polyductin

Gene names

    • Name
      PKHD1

Organism names

Accessions

  • Primary accession
    E2RK30

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Single-pass membrane protein
Cytoplasm
Apical cell membrane
Nucleus
Secreted
Endoplasmic reticulum
Golgi apparatus
Note: The intra-cellular C-terminal fragment (ICD) translocates to the nucleus and is not detected in primary cilia (By similarity).
The extracellular domain (PECD) traffics beyond the mid-Golgi and localizes on exosome like vesicles (ELVs) attached to the primary cilium (By similarity).
In the urine, the extracellular domain (PECD) exists as a highly abundant secreted form and a less abundant PECD form that is either tethered to or shed with the C-terminal fragment (PTM) in ELVs (By similarity).
The majority of full length PKHD1 protein resides at the endoplasmic reticulum and cannot pass beyond the mid-Golgi apparatus and is not detected in primary cilia (By similarity).
The intra-cellular C-terminal fragment of 21-kDa translocates to the nucleus. The extracellular domain traffics beyond the mid-Golgi and localizes on exosome like vesicles (ELVs) attached to the primary cilium (By similarity).

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane3854-3874Helical

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-22
ChainPRO_500316362123-4074Fibrocystin
Glycosylation54N-linked (GlcNAc...) asparagine
Glycosylation224N-linked (GlcNAc...) asparagine
Glycosylation355N-linked (GlcNAc...) asparagine
Glycosylation385N-linked (GlcNAc...) asparagine
Glycosylation518N-linked (GlcNAc...) asparagine
Glycosylation527N-linked (GlcNAc...) asparagine
Glycosylation640N-linked (GlcNAc...) asparagine
Glycosylation710N-linked (GlcNAc...) asparagine
Glycosylation741N-linked (GlcNAc...) asparagine
Glycosylation822N-linked (GlcNAc...) asparagine
Glycosylation829N-linked (GlcNAc...) asparagine
Glycosylation868N-linked (GlcNAc...) asparagine
Glycosylation953N-linked (GlcNAc...) asparagine
Glycosylation966N-linked (GlcNAc...) asparagine
Glycosylation976N-linked (GlcNAc...) asparagine
Glycosylation1006N-linked (GlcNAc...) asparagine
Glycosylation1059N-linked (GlcNAc...) asparagine
Glycosylation1083N-linked (GlcNAc...) asparagine
Glycosylation1115N-linked (GlcNAc...) asparagine
Glycosylation1134N-linked (GlcNAc...) asparagine
Glycosylation1233N-linked (GlcNAc...) asparagine
Glycosylation1240N-linked (GlcNAc...) asparagine
Glycosylation1274N-linked (GlcNAc...) asparagine
Glycosylation1284N-linked (GlcNAc...) asparagine
Glycosylation1308N-linked (GlcNAc...) asparagine
Glycosylation1319N-linked (GlcNAc...) asparagine
Glycosylation1342N-linked (GlcNAc...) asparagine
Glycosylation1373N-linked (GlcNAc...) asparagine
Glycosylation1445N-linked (GlcNAc...) asparagine
Glycosylation1456N-linked (GlcNAc...) asparagine
Glycosylation1471N-linked (GlcNAc...) asparagine
Glycosylation1490N-linked (GlcNAc...) asparagine
Glycosylation1528N-linked (GlcNAc...) asparagine
Glycosylation1560N-linked (GlcNAc...) asparagine
Glycosylation1578N-linked (GlcNAc...) asparagine
Glycosylation1598N-linked (GlcNAc...) asparagine
Glycosylation1627N-linked (GlcNAc...) asparagine
Glycosylation1694N-linked (GlcNAc...) asparagine
Glycosylation1760N-linked (GlcNAc...) asparagine
Glycosylation1775N-linked (GlcNAc...) asparagine
Glycosylation1789N-linked (GlcNAc...) asparagine
Glycosylation1875N-linked (GlcNAc...) asparagine
Glycosylation1915N-linked (GlcNAc...) asparagine
Glycosylation1941N-linked (GlcNAc...) asparagine
Glycosylation1955N-linked (GlcNAc...) asparagine
Glycosylation2030N-linked (GlcNAc...) asparagine
Glycosylation2111N-linked (GlcNAc...) asparagine
Glycosylation2140N-linked (GlcNAc...) asparagine
Glycosylation2390N-linked (GlcNAc...) asparagine
Glycosylation2431N-linked (GlcNAc...) asparagine
Glycosylation2467N-linked (GlcNAc...) asparagine
Glycosylation2531N-linked (GlcNAc...) asparagine
Glycosylation2549N-linked (GlcNAc...) asparagine
Glycosylation2579N-linked (GlcNAc...) asparagine
Glycosylation2591N-linked (GlcNAc...) asparagine
Glycosylation2749N-linked (GlcNAc...) asparagine
Glycosylation2764N-linked (GlcNAc...) asparagine
Glycosylation2972N-linked (GlcNAc...) asparagine
Glycosylation3004N-linked (GlcNAc...) asparagine
Glycosylation3053N-linked (GlcNAc...) asparagine
Glycosylation3136N-linked (GlcNAc...) asparagine
Glycosylation3165N-linked (GlcNAc...) asparagine
Glycosylation3221N-linked (GlcNAc...) asparagine
Glycosylation3484N-linked (GlcNAc...) asparagine
Glycosylation3702N-linked (GlcNAc...) asparagine
Glycosylation3721N-linked (GlcNAc...) asparagine
Glycosylation3833N-linked (GlcNAc...) asparagine

Post-translational modification

Palmitoylated. Palmitoylation facilitates the trafficking to the cilia and membrane targeting.
N-glycosylated.
Several proteolytic cleavages occur within the extracellular domain, whereas at least one cleavage occurs within the cytoplasmic domain. Cleaved by a probable proprotein convertase which produces an extracellular domain (polyductin extracellular domain, (PECD)) and a C-terminal fragment (polyductin transmembrane fragment (PTM)) which are tethered together by disulfide bonds. This extracellular domain (PECD) is then shed from the primary cilium by activation of a member of the ADAM metalloproteinase disintegrins family, resulting in concomitant release of an intra-cellular C-terminal fragment (ICD) via a gamma-secretase-dependent process. The proteolytic cleavage of the C-terminal intracellular fragment (ICD) is controlled by cytosolic calcium concentration and activation of PKC.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with CAMLG. Interacts with PKD2. Interacts (via CST) with ARF4; this interaction allows an efficient PKHD1 trafficking to the cilium. Interacts (via CST) with RAB8A; this interaction controls trafficking through the endomembrane systeme and to the cilium. Interacts (via CST) with TULP3; this interaction allows PKHD1 trafficking to the cilium.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, repeat, region, compositional bias.

TypeIDPosition(s)Description
Domain258-310IPT/TIG 1
Domain323-483PA14
Domain944-1000IPT/TIG 2
Domain1018-1101IPT/TIG 3
Domain1107-1186IPT/TIG 4
Domain1199-1274IPT/TIG 5
Domain1385-1464IPT/TIG 6
Domain1573-1641IPT/TIG 7
Domain1928-2049G8 1
Repeat2245-2267PbH1 1
Repeat2288-2322PbH1 2
Repeat2351-2373PbH1 3
Repeat2383-2404PbH1 4
Repeat2405-2427PbH1 5
Repeat2460-2483PbH1 6
Domain2743-2869G8 2
Repeat3029-3051PbH1 7
Repeat3082-3104PbH1 8
Repeat3158-3183PbH1 9
Region3871-3888Ciliary targeting sequence (CST)
Region3896-3919Disordered
Region3943-3965Disordered
Region3947-3976Nuclear localization signal (NLS)
Compositional bias3950-3965Basic and acidic residues
Region4031-4074Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    4,074
  • Mass (Da)
    447,576
  • Last updated
    2012-10-31 v2
  • Checksum
    173062C7FA7FC244

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias3950-3965Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAEX03008386
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAEX03008387
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAEX03008388
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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