PKD2_CAEEL
ID PKD2_CAEEL Reviewed; 716 AA.
AC Q9U1S7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Polycystin-2 {ECO:0000303|PubMed:15862350};
DE Short=CePc2;
DE AltName: Full=Polycystic kidney disease 2 protein homolog {ECO:0000250|UniProtKB:Q13563};
GN Name=pkd-2 {ECO:0000312|WormBase:Y73F8A.1};
GN Synonyms=pdk-2 {ECO:0000312|WormBase:Y73F8A.1};
GN ORFNames=Y73F8A.1 {ECO:0000312|WormBase:Y73F8A.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CAB60565.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB60565.3};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=10517638; DOI=10.1038/43913;
RA Barr M.M., Sternberg P.W.;
RT "A polycystic kidney-disease gene homologue required for male mating
RT behaviour in C. elegans.";
RL Nature 401:386-389(1999).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11553327; DOI=10.1016/s0960-9822(01)00423-7;
RA Barr M.M., DeModena J., Braun D., Nguyen C.Q., Hall D.H., Sternberg P.W.;
RT "The Caenorhabditis elegans autosomal dominant polycystic kidney disease
RT gene homologs lov-1 and pkd-2 act in the same pathway.";
RL Curr. Biol. 11:1341-1346(2001).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12411744; DOI=10.1159/000066650;
RA Kaletta T., Van der Craen M., Van Geel A., Dewulf N., Bogaert T.,
RA Branden M., King K.V., Buechner M., Barstead R., Hyink D., Li H.-P.,
RA Geng L., Burrow C., Wilson P.;
RT "Towards understanding the polycystins.";
RL Nephron Exp. Nephrol. 93:E9-17(2003).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=15862350; DOI=10.1016/j.ceca.2005.03.003;
RA Koulen P., Duncan R.S., Liu J., Cohen N.E., Yannazzo J.-A.S., McClung N.,
RA Lockhart C.L., Branden M., Buechner M.;
RT "Polycystin-2 accelerates Ca2+ release from intracellular stores in
RT Caenorhabditis elegans.";
RL Cell Calcium 37:593-601(2005).
RN [6] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15753033; DOI=10.1016/j.cub.2004.12.073;
RA Peden E.M., Barr M.M.;
RT "The KLP-6 kinesin is required for male mating behaviors and polycystin
RT localization in Caenorhabditis elegans.";
RL Curr. Biol. 15:394-404(2005).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15563610; DOI=10.1091/mbc.e04-09-0851;
RA Hu J., Barr M.M.;
RT "ATP-2 interacts with the PLAT domain of LOV-1 and is involved in
RT Caenorhabditis elegans polycystin signaling.";
RL Mol. Biol. Cell 16:458-469(2005).
RN [8] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16943275; DOI=10.1242/dev.02555;
RA Bae Y.-K., Qin H., Knobel K.M., Hu J., Rosenbaum J.L., Barr M.M.;
RT "General and cell-type specific mechanisms target TRPP2/PKD-2 to cilia.";
RL Development 133:3859-3870(2006).
RN [9] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-534,
RP DEPHOSPHORYLATION BY CALCINEURIN, AND MUTAGENESIS OF SER-534.
RX PubMed=16481400; DOI=10.1091/mbc.e05-10-0935;
RA Hu J., Bae Y.-K., Knobel K.M., Barr M.M.;
RT "Casein kinase II and calcineurin modulate TRPP function and ciliary
RT localization.";
RL Mol. Biol. Cell 17:2200-2211(2006).
RN [10] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-534.
RX PubMed=17581863; DOI=10.1091/mbc.e07-03-0239;
RA Hu J., Wittekind S.G., Barr M.M.;
RT "STAM and Hrs down-regulate ciliary TRP receptors.";
RL Mol. Biol. Cell 18:3277-3289(2007).
RN [11] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=18037411; DOI=10.1016/j.yexcr.2007.10.017;
RA Knobel K.M., Peden E.M., Barr M.M.;
RT "Distinct protein domains regulate ciliary targeting and function of C.
RT elegans PKD-2.";
RL Exp. Cell Res. 314:825-833(2008).
RN [12]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-534.
RX PubMed=26150102; DOI=10.1038/srep11855;
RA Xu Q., Zhang Y., Wei Q., Huang Y., Li Y., Ling K., Hu J.;
RT "BBS4 and BBS5 show functional redundancy in the BBSome to regulate the
RT degradative sorting of ciliary sensory receptors.";
RL Sci. Rep. 5:11855-11855(2015).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28745435; DOI=10.1002/cm.21387;
RA Piasecki B.P., Sasani T.A., Lessenger A.T., Huth N., Farrell S.;
RT "MAPK-15 is a ciliary protein required for PKD-2 localization and male
RT mating behavior in Caenorhabditis elegans.";
RL Cytoskeleton 74:390-402(2017).
RN [14]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=31264582; DOI=10.7554/elife.43660;
RA Lawson H., Vuong E., Miller R.M., Kiontke K., Fitch D.H., Portman D.S.;
RT "The Makorin lep-2 and the lncRNA lep-5 regulate lin-28 to schedule sexual
RT maturation of the C. elegans nervous system.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Functions as a calcium permeable cation channel
CC (PubMed:15862350). Required for 2 aspects of male mating behavior:
CC response to hermaphrodite contact and vulva location (PubMed:11553327,
CC PubMed:12411744, PubMed:15862350, PubMed:15753033, PubMed:18037411,
CC PubMed:28745435). Acts in the same pathway as lov-1 and atp-2 in
CC response behavior (PubMed:11553327). {ECO:0000269|PubMed:11553327,
CC ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15753033,
CC ECO:0000269|PubMed:15862350, ECO:0000269|PubMed:18037411,
CC ECO:0000269|PubMed:28745435}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11553327,
CC ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15563610,
CC ECO:0000269|PubMed:15753033, ECO:0000269|PubMed:16481400,
CC ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:17581863,
CC ECO:0000269|PubMed:18037411}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11553327, ECO:0000269|PubMed:12411744,
CC ECO:0000269|PubMed:15563610, ECO:0000269|PubMed:15753033,
CC ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:16943275,
CC ECO:0000269|PubMed:17581863, ECO:0000269|PubMed:18037411}. Cell
CC projection, cilium membrane {ECO:0000269|PubMed:11553327,
CC ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15563610,
CC ECO:0000269|PubMed:15753033, ECO:0000269|PubMed:16481400,
CC ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:17581863,
CC ECO:0000269|PubMed:18037411}. Cell projection, cilium
CC {ECO:0000269|PubMed:11553327, ECO:0000269|PubMed:12411744,
CC ECO:0000269|PubMed:15563610, ECO:0000269|PubMed:15753033,
CC ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:16943275,
CC ECO:0000269|PubMed:17581863, ECO:0000269|PubMed:18037411,
CC ECO:0000269|PubMed:26150102, ECO:0000269|PubMed:28745435}. Cell
CC projection, axon {ECO:0000269|PubMed:11553327,
CC ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15563610,
CC ECO:0000269|PubMed:15753033, ECO:0000269|PubMed:16481400,
CC ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:17581863,
CC ECO:0000269|PubMed:18037411}. Cell projection, dendrite
CC {ECO:0000269|PubMed:11553327, ECO:0000269|PubMed:12411744,
CC ECO:0000269|PubMed:15563610, ECO:0000269|PubMed:15753033,
CC ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:16943275,
CC ECO:0000269|PubMed:17581863, ECO:0000269|PubMed:18037411}. Perikaryon
CC {ECO:0000269|PubMed:11553327, ECO:0000269|PubMed:12411744,
CC ECO:0000269|PubMed:15563610, ECO:0000269|PubMed:15753033,
CC ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:16943275,
CC ECO:0000269|PubMed:17581863, ECO:0000269|PubMed:18037411}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:11553327,
CC ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15563610,
CC ECO:0000269|PubMed:15753033, ECO:0000269|PubMed:16481400,
CC ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:17581863,
CC ECO:0000269|PubMed:18037411}. Note=Synthesized in the endoplasmic
CC reticulum, and then packaged into vesicles that are transported to the
CC ciliary base and inserted into the ciliary membrane. Localizes to both
CC the ciliary base and cilium proper. {ECO:0000269|PubMed:11553327,
CC ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15563610,
CC ECO:0000269|PubMed:15753033, ECO:0000269|PubMed:16481400,
CC ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:17581863,
CC ECO:0000269|PubMed:18037411}.
CC -!- TISSUE SPECIFICITY: Exclusively expressed in a subset of 3 categories
CC of adult male sensory neurons: ray neurons, hook neurons and head
CC cephalic (CEM) neurons (PubMed:10517638, PubMed:11553327,
CC PubMed:12411744, PubMed:15563610, PubMed:16943275, PubMed:16481400,
CC PubMed:31264582). Expressed in the male tail (PubMed:26150102,
CC PubMed:28745435). {ECO:0000269|PubMed:10517638,
CC ECO:0000269|PubMed:11553327, ECO:0000269|PubMed:12411744,
CC ECO:0000269|PubMed:15563610, ECO:0000269|PubMed:16481400,
CC ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:26150102,
CC ECO:0000269|PubMed:28745435, ECO:0000269|PubMed:31264582}.
CC -!- DEVELOPMENTAL STAGE: First expressed during L4 and peaks in the adult
CC male. {ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:31264582}.
CC -!- DOMAIN: The transmembrane domains are sufficient for localization in
CC the cilium. The cytoplasmic tails are necessary for localization in
CC cell bodies and anchoring at the ciliary base. Cytoplasmic tails also
CC regulate sensory function. {ECO:0000269|PubMed:18037411}.
CC -!- PTM: Phosphorylated. CK2 (kin-3 and kin-10) and calcineurin act
CC antagonistically to regulate the phosphorylation state.
CC {ECO:0000269|PubMed:16481400}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit defects in 2 aspects of male mating
CC behavior: response to hermaphrodite contact and vulva location.
CC {ECO:0000269|PubMed:11553327, ECO:0000269|PubMed:28745435}.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000255}.
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DR EMBL; BX284604; CAB60565.3; -; Genomic_DNA.
DR RefSeq; NP_502838.3; NM_070437.4.
DR AlphaFoldDB; Q9U1S7; -.
DR SMR; Q9U1S7; -.
DR BioGRID; 43506; 1.
DR ComplexPortal; CPX-3887; TRPP complex.
DR IntAct; Q9U1S7; 4.
DR MINT; Q9U1S7; -.
DR STRING; 6239.Y73F8A.1; -.
DR TCDB; 1.A.5.2.4; the polycystin cation channel (pcc) family.
DR iPTMnet; Q9U1S7; -.
DR PaxDb; Q9U1S7; -.
DR PeptideAtlas; Q9U1S7; -.
DR EnsemblMetazoa; Y73F8A.1.1; Y73F8A.1.1; WBGene00004035.
DR GeneID; 178424; -.
DR KEGG; cel:CELE_Y73F8A.1; -.
DR UCSC; Y73F8A.1; c. elegans.
DR CTD; 178424; -.
DR WormBase; Y73F8A.1; CE38663; WBGene00004035; pkd-2.
DR eggNOG; KOG3599; Eukaryota.
DR GeneTree; ENSGT00880000138223; -.
DR HOGENOM; CLU_012097_0_0_1; -.
DR InParanoid; Q9U1S7; -.
DR OMA; YYIIEET; -.
DR OrthoDB; 426073at2759; -.
DR PhylomeDB; Q9U1S7; -.
DR Reactome; R-CEL-5620916; VxPx cargo-targeting to cilium.
DR PRO; PR:Q9U1S7; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004035; Expressed in material anatomical entity and 2 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0031090; C:organelle membrane; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0071683; C:sensory dendrite; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
DR GO; GO:0060179; P:male mating behavior; IDA:UniProtKB.
DR GO; GO:0007617; P:mating behavior; IMP:WormBase.
DR GO; GO:0023041; P:neuronal signal transduction; IC:WormBase.
DR GO; GO:1902435; P:regulation of male mating behavior; IC:ComplexPortal.
DR GO; GO:0034606; P:response to hermaphrodite contact; IMP:UniProtKB.
DR GO; GO:0034608; P:vulval location; IMP:UniProtKB.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR003915; PKD_2.
DR Pfam; PF08016; PKD_channel; 1.
DR PRINTS; PR01433; POLYCYSTIN2.
PE 1: Evidence at protein level;
KW Behavior; Cell membrane; Cell projection; Cilium; Coiled coil;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc.
FT CHAIN 1..716
FT /note="Polycystin-2"
FT /id="PRO_0000347285"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..409
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 483..497
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TOPO_DOM 498..510
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 613..680
FT /evidence="ECO:0000255"
FT COMPBIAS 27..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 534
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:16481400"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 180..193
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT MUTAGEN 534
FT /note="S->A: Fails to rescue pkd-2 defects. Prevents
FT phosphorylation at this site."
FT /evidence="ECO:0000269|PubMed:16481400,
FT ECO:0000269|PubMed:17581863"
FT MUTAGEN 534
FT /note="S->D: Phospho-mimetic. Acts as if constitutively
FT phosphorylated."
FT /evidence="ECO:0000269|PubMed:16481400,
FT ECO:0000269|PubMed:17581863, ECO:0000269|PubMed:26150102"
SQ SEQUENCE 716 AA; 80435 MW; 8264460CBC904282 CRC64;
MNYGAADERW ANPPQPVAAA EHGPSFDHSM VSEEYEHDKK KNPAQKEGIS FSQALLASGH
EKSDGKIKLT ARSFMEVGGY AVFLIVLVYV AFAQNSIQSY YYSKVMSDLF VASTGASGAP
AFGSCTSMDN IWDWLSQVLI PGIYWTETSN STDNENMIYY ENRLLGEPRI RMLKVTNDSC
TVMKSFQREI KECFANYEEK LEDKTMVGDG SVDAFIYATA KELENLKTVG TIASYGGGGF
VQRLPVAGST EAQSAIATLK ANRWIDRGSR AIIVDFALYN ANINLFCVVK LLFELPASGG
VITTPKLMTY DLLTYQTSGG TRMMIFEGIF CGFILYFIFE ELFAIGRHRL HYLTQFWNLV
DVVLLGFSVA TIILSVNRTK TGVNRVNSVI ENGLTNAPFD DVTSSENSYL NIKACVVFVA
WVKVFKFISV NKTMSQLSST LTRSAKDIGG FAVMFAVFFF AFAQFGYLCF GTQIADYSNL
YNSAFALLRL ILGDFNFSAL ESCNRFFGPA FFIAYVFFVS FILLNMFLAI INDSYVEVKA
ELARKKDGEG ILDWFMNKVR GLTKRGKRPD APGEDATYED YKLMLYRAGY AEKDINEAFT
RFNVTSMTEH VPEKVAEDIA DEVARMTEQK RNYMENHRDY ANLNRRVDQM QESVFSIVDR
IEGVNATLQT IEKQRVQQQD GGNLMDLSAL LTNQVRNRES AARRPTITSI ADKKEE
