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Protein

Polycystin-2

Gene

pkd-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a calcium permeable cation channel. Required for 2 aspects of male mating behavior: response to hermaphrodite contact and vulva location. Acts in the same pathway as lov-1 and atp-2 in response behavior.5 Publications

GO - Molecular functioni

  • calcium channel activity Source: UniProtKB
  • calcium ion binding Source: InterPro

GO - Biological processi

  • calcium ion transport Source: UniProtKB
  • detection of mechanical stimulus Source: GO_Central
  • male mating behavior Source: UniProtKB
  • mating behavior Source: WormBase
  • neuronal signal transduction Source: WormBase
  • response to hermaphrodite contact Source: UniProtKB
  • vulval location Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Behavior, Ion transport, Transport

Keywords - Ligandi

Zinc

Protein family/group databases

TCDBi1.A.5.2.4. the polycystin cation channel (pcc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Polycystin-21 Publication
Short name:
CePc2
Alternative name(s):
Polycystic kidney disease 2 protein homologBy similarity
Gene namesi
Name:pkd-2Imported
ORF Names:Y73F8A.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiY73F8A.1; CE38663; WBGene00004035; pkd-2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 72CytoplasmicSequence analysisAdd BLAST72
Transmembranei73 – 93HelicalSequence analysisAdd BLAST21
Topological domaini94 – 324ExtracellularSequence analysisAdd BLAST231
Transmembranei325 – 345HelicalSequence analysisAdd BLAST21
Topological domaini346 – 355CytoplasmicSequence analysis10
Transmembranei356 – 376HelicalSequence analysisAdd BLAST21
Topological domaini377 – 409ExtracellularSequence analysisAdd BLAST33
Transmembranei410 – 430HelicalSequence analysisAdd BLAST21
Topological domaini431 – 447CytoplasmicSequence analysisAdd BLAST17
Transmembranei448 – 468HelicalSequence analysisAdd BLAST21
Topological domaini469 – 510ExtracellularSequence analysisAdd BLAST42
Transmembranei511 – 531HelicalSequence analysisAdd BLAST21
Topological domaini532 – 716CytoplasmicSequence analysisAdd BLAST185

GO - Cellular componenti

  • axon Source: WormBase
  • ciliary membrane Source: UniProtKB
  • cilium Source: UniProtKB
  • dendrite Source: WormBase
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • non-motile cilium Source: WormBase
  • organelle membrane Source: WormBase
  • perikaryon Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: WormBase
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Worms exhibit defects in 2 aspects of male mating behavior: response to hermaphrodite contact and vulva location.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi534S → A: Fails to rescue pkd-2 defects. Prevents phosphorylation at this site. 2 Publications1
Mutagenesisi534S → D: Phospho-mimetic. Acts as if constitutively phosphorylated. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003472851 – 716Polycystin-2Add BLAST716

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi150N-linked (GlcNAc...)Sequence analysis1
Glycosylationi177N-linked (GlcNAc...)Sequence analysis1
Glycosylationi377N-linked (GlcNAc...)Sequence analysis1
Glycosylationi496N-linked (GlcNAc...)Sequence analysis1
Modified residuei534Phosphoserine; by CK21 Publication1

Post-translational modificationi

Phosphorylated. CK2 (kin-3 and kin-10) and calcineurin act antagonistically to regulate the phosphorylation state.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9U1S7.
PeptideAtlasiQ9U1S7.

PTM databases

iPTMnetiQ9U1S7.

Expressioni

Tissue specificityi

Exclusively expressed in a subset of 3 categories of adult male sensory neurons: ray neurons, hook neurons and head cephalic (CEM) neurons (PubMed:10517638, PubMed:11553327, PubMed:12411744, PubMed:15563610, PubMed:16943275, PubMed:16481400). Expressed in the male tail (PubMed:26150102).7 Publications

Developmental stagei

First expressed during L4 and peaks in the adult male.1 Publication

Gene expression databases

BgeeiWBGene00004035.

Interactioni

Protein-protein interaction databases

IntActiQ9U1S7. 4 interactors.
MINTiMINT-3385171.
STRINGi6239.Y73F8A.1.

Structurei

3D structure databases

ProteinModelPortaliQ9U1S7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili613 – 680Sequence analysisAdd BLAST68

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi165 – 177Polycystin motifSequence analysisAdd BLAST13

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi451 – 527Phe-richSequence analysisAdd BLAST77

Domaini

The transmembrane domains are sufficient for localization in the cilium. The cytoplasmic tails are necessary for localization in cell bodies and anchoring at the ciliary base. Cytoplasmic tails also regulate sensory function.1 Publication

Sequence similaritiesi

Belongs to the polycystin family.Sequence analysis

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3599. Eukaryota.
ENOG410XTGE. LUCA.
GeneTreeiENSGT00700000104221.
HOGENOMiHOG000230858.
InParanoidiQ9U1S7.
KOiK04986.
OMAiKRRETMG.
OrthoDBiEOG091G034F.
PhylomeDBiQ9U1S7.

Family and domain databases

InterProiIPR013122. PKD1_2_channel.
IPR003915. PKD_2.
[Graphical view]
PfamiPF08016. PKD_channel. 1 hit.
[Graphical view]
PRINTSiPR01433. POLYCYSTIN2.

Sequencei

Sequence statusi: Complete.

Q9U1S7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYGAADERW ANPPQPVAAA EHGPSFDHSM VSEEYEHDKK KNPAQKEGIS
60 70 80 90 100
FSQALLASGH EKSDGKIKLT ARSFMEVGGY AVFLIVLVYV AFAQNSIQSY
110 120 130 140 150
YYSKVMSDLF VASTGASGAP AFGSCTSMDN IWDWLSQVLI PGIYWTETSN
160 170 180 190 200
STDNENMIYY ENRLLGEPRI RMLKVTNDSC TVMKSFQREI KECFANYEEK
210 220 230 240 250
LEDKTMVGDG SVDAFIYATA KELENLKTVG TIASYGGGGF VQRLPVAGST
260 270 280 290 300
EAQSAIATLK ANRWIDRGSR AIIVDFALYN ANINLFCVVK LLFELPASGG
310 320 330 340 350
VITTPKLMTY DLLTYQTSGG TRMMIFEGIF CGFILYFIFE ELFAIGRHRL
360 370 380 390 400
HYLTQFWNLV DVVLLGFSVA TIILSVNRTK TGVNRVNSVI ENGLTNAPFD
410 420 430 440 450
DVTSSENSYL NIKACVVFVA WVKVFKFISV NKTMSQLSST LTRSAKDIGG
460 470 480 490 500
FAVMFAVFFF AFAQFGYLCF GTQIADYSNL YNSAFALLRL ILGDFNFSAL
510 520 530 540 550
ESCNRFFGPA FFIAYVFFVS FILLNMFLAI INDSYVEVKA ELARKKDGEG
560 570 580 590 600
ILDWFMNKVR GLTKRGKRPD APGEDATYED YKLMLYRAGY AEKDINEAFT
610 620 630 640 650
RFNVTSMTEH VPEKVAEDIA DEVARMTEQK RNYMENHRDY ANLNRRVDQM
660 670 680 690 700
QESVFSIVDR IEGVNATLQT IEKQRVQQQD GGNLMDLSAL LTNQVRNRES
710
AARRPTITSI ADKKEE
Length:716
Mass (Da):80,435
Last modified:June 7, 2005 - v3
Checksum:i8264460CBC904282
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132862 Genomic DNA. Translation: CAB60565.3.
RefSeqiNP_502838.3. NM_070437.4.
UniGeneiCel.12535.

Genome annotation databases

EnsemblMetazoaiY73F8A.1; Y73F8A.1; WBGene00004035.
GeneIDi178424.
KEGGicel:CELE_Y73F8A.1.
UCSCiY73F8A.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132862 Genomic DNA. Translation: CAB60565.3.
RefSeqiNP_502838.3. NM_070437.4.
UniGeneiCel.12535.

3D structure databases

ProteinModelPortaliQ9U1S7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9U1S7. 4 interactors.
MINTiMINT-3385171.
STRINGi6239.Y73F8A.1.

Protein family/group databases

TCDBi1.A.5.2.4. the polycystin cation channel (pcc) family.

PTM databases

iPTMnetiQ9U1S7.

Proteomic databases

PaxDbiQ9U1S7.
PeptideAtlasiQ9U1S7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY73F8A.1; Y73F8A.1; WBGene00004035.
GeneIDi178424.
KEGGicel:CELE_Y73F8A.1.
UCSCiY73F8A.1. c. elegans.

Organism-specific databases

CTDi178424.
WormBaseiY73F8A.1; CE38663; WBGene00004035; pkd-2.

Phylogenomic databases

eggNOGiKOG3599. Eukaryota.
ENOG410XTGE. LUCA.
GeneTreeiENSGT00700000104221.
HOGENOMiHOG000230858.
InParanoidiQ9U1S7.
KOiK04986.
OMAiKRRETMG.
OrthoDBiEOG091G034F.
PhylomeDBiQ9U1S7.

Miscellaneous databases

PROiQ9U1S7.

Gene expression databases

BgeeiWBGene00004035.

Family and domain databases

InterProiIPR013122. PKD1_2_channel.
IPR003915. PKD_2.
[Graphical view]
PfamiPF08016. PKD_channel. 1 hit.
[Graphical view]
PRINTSiPR01433. POLYCYSTIN2.
ProtoNetiSearch...

Entry informationi

Entry nameiPKD2_CAEEL
AccessioniPrimary (citable) accession number: Q9U1S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: June 7, 2005
Last modified: November 30, 2016
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.