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Polycystin-2 (CePc2) (Polycystic kidney disease 2 protein homolog)

 PKD2_CAEEL              Reviewed;         716 AA.
Q9U1S7;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 3.
25-OCT-2017, entry version 109.
RecName: Full=Polycystin-2 {ECO:0000303|PubMed:15862350};
Short=CePc2;
AltName: Full=Polycystic kidney disease 2 protein homolog {ECO:0000250|UniProtKB:Q13563};
Name=pkd-2 {ECO:0000312|EMBL:CAB60565.3}; ORFNames=Y73F8A.1;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000312|EMBL:CAB60565.3}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB60565.3};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000305}
TISSUE SPECIFICITY.
PubMed=10517638; DOI=10.1038/43916;
Barr M.M., Sternberg P.W.;
"A polycystic kidney-disease gene homologue required for male mating
behaviour in C. elegans.";
Nature 401:386-389(1999).
[3] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=11553327; DOI=10.1016/S0960-9822(01)00423-7;
Barr M.M., DeModena J., Braun D., Nguyen C.Q., Hall D.H.,
Sternberg P.W.;
"The Caenorhabditis elegans autosomal dominant polycystic kidney
disease gene homologs lov-1 and pkd-2 act in the same pathway.";
Curr. Biol. 11:1341-1346(2001).
[4] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=12411744;
Kaletta T., Van der Craen M., Van Geel A., Dewulf N., Bogaert T.,
Branden M., King K.V., Buechner M., Barstead R., Hyink D., Li H.-P.,
Geng L., Burrow C., Wilson P.;
"Towards understanding the polycystins.";
Nephron Exp. Nephrol. 93:E9-17(2003).
[5] {ECO:0000305}
FUNCTION.
PubMed=15862350; DOI=10.1016/j.ceca.2005.03.003;
Koulen P., Duncan R.S., Liu J., Cohen N.E., Yannazzo J.-A.S.,
McClung N., Lockhart C.L., Branden M., Buechner M.;
"Polycystin-2 accelerates Ca2+ release from intracellular stores in
Caenorhabditis elegans.";
Cell Calcium 37:593-601(2005).
[6] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15753033; DOI=10.1016/j.cub.2004.12.073;
Peden E.M., Barr M.M.;
"The KLP-6 kinesin is required for male mating behaviors and
polycystin localization in Caenorhabditis elegans.";
Curr. Biol. 15:394-404(2005).
[7] {ECO:0000305}
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15563610; DOI=10.1091/mbc.E04-09-0851;
Hu J., Barr M.M.;
"ATP-2 interacts with the PLAT domain of LOV-1 and is involved in
Caenorhabditis elegans polycystin signaling.";
Mol. Biol. Cell 16:458-469(2005).
[8] {ECO:0000305}
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16943275; DOI=10.1242/dev.02555;
Bae Y.-K., Qin H., Knobel K.M., Hu J., Rosenbaum J.L., Barr M.M.;
"General and cell-type specific mechanisms target TRPP2/PKD-2 to
cilia.";
Development 133:3859-3870(2006).
[9] {ECO:0000305}
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-534,
DEPHOSPHORYLATION BY CALCINEURIN, AND MUTAGENESIS OF SER-534.
PubMed=16481400; DOI=10.1091/mbc.E05-10-0935;
Hu J., Bae Y.-K., Knobel K.M., Barr M.M.;
"Casein kinase II and calcineurin modulate TRPP function and ciliary
localization.";
Mol. Biol. Cell 17:2200-2211(2006).
[10] {ECO:0000305}
SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-534.
PubMed=17581863; DOI=10.1091/mbc.E07-03-0239;
Hu J., Wittekind S.G., Barr M.M.;
"STAM and Hrs down-regulate ciliary TRP receptors.";
Mol. Biol. Cell 18:3277-3289(2007).
[11] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=18037411; DOI=10.1016/j.yexcr.2007.10.017;
Knobel K.M., Peden E.M., Barr M.M.;
"Distinct protein domains regulate ciliary targeting and function of
C. elegans PKD-2.";
Exp. Cell Res. 314:825-833(2008).
[12]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-534.
PubMed=26150102; DOI=10.1038/srep11855;
Xu Q., Zhang Y., Wei Q., Huang Y., Li Y., Ling K., Hu J.;
"BBS4 and BBS5 show functional redundancy in the BBSome to regulate
the degradative sorting of ciliary sensory receptors.";
Sci. Rep. 5:11855-11855(2015).
[13]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=28745435; DOI=10.1002/cm.21387;
Piasecki B.P., Sasani T.A., Lessenger A.T., Huth N., Farrell S.;
"MAPK-15 is a ciliary protein required for PKD-2 localization and male
mating behavior in Caenorhabditis elegans.";
Cytoskeleton 0:0-0(2017).
-!- FUNCTION: Functions as a calcium permeable cation channel
(PubMed:15862350). Required for 2 aspects of male mating behavior:
response to hermaphrodite contact and vulva location
(PubMed:11553327, PubMed:12411744, PubMed:15862350,
PubMed:15753033, PubMed:18037411, PubMed:28745435). Acts in the
same pathway as lov-1 and atp-2 in response behavior
(PubMed:11553327). {ECO:0000269|PubMed:11553327,
ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15753033,
ECO:0000269|PubMed:15862350, ECO:0000269|PubMed:18037411,
ECO:0000269|PubMed:28745435}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11553327,
ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15563610,
ECO:0000269|PubMed:15753033, ECO:0000269|PubMed:16481400,
ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:17581863,
ECO:0000269|PubMed:18037411}; Multi-pass membrane protein
{ECO:0000269|PubMed:11553327, ECO:0000269|PubMed:12411744,
ECO:0000269|PubMed:15563610, ECO:0000269|PubMed:15753033,
ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:16943275,
ECO:0000269|PubMed:17581863, ECO:0000269|PubMed:18037411}. Cell
projection, cilium membrane {ECO:0000269|PubMed:11553327,
ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15563610,
ECO:0000269|PubMed:15753033, ECO:0000269|PubMed:16481400,
ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:17581863,
ECO:0000269|PubMed:18037411}. Cell projection, cilium
{ECO:0000269|PubMed:11553327, ECO:0000269|PubMed:12411744,
ECO:0000269|PubMed:15563610, ECO:0000269|PubMed:15753033,
ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:16943275,
ECO:0000269|PubMed:17581863, ECO:0000269|PubMed:18037411,
ECO:0000269|PubMed:26150102, ECO:0000269|PubMed:28745435}. Cell
projection, axon {ECO:0000269|PubMed:11553327,
ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15563610,
ECO:0000269|PubMed:15753033, ECO:0000269|PubMed:16481400,
ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:17581863,
ECO:0000269|PubMed:18037411}. Cell projection, dendrite
{ECO:0000269|PubMed:11553327, ECO:0000269|PubMed:12411744,
ECO:0000269|PubMed:15563610, ECO:0000269|PubMed:15753033,
ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:16943275,
ECO:0000269|PubMed:17581863, ECO:0000269|PubMed:18037411}.
Perikaryon {ECO:0000269|PubMed:11553327,
ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15563610,
ECO:0000269|PubMed:15753033, ECO:0000269|PubMed:16481400,
ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:17581863,
ECO:0000269|PubMed:18037411}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:11553327, ECO:0000269|PubMed:12411744,
ECO:0000269|PubMed:15563610, ECO:0000269|PubMed:15753033,
ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:16943275,
ECO:0000269|PubMed:17581863, ECO:0000269|PubMed:18037411}.
Note=Synthesized in the endoplasmic reticulum, and then packaged
into vesicles that are transported to the ciliary base and
inserted into the ciliary membrane. Localizes to both the ciliary
base and cilium proper. {ECO:0000269|PubMed:11553327,
ECO:0000269|PubMed:12411744, ECO:0000269|PubMed:15563610,
ECO:0000269|PubMed:15753033, ECO:0000269|PubMed:16481400,
ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:17581863,
ECO:0000269|PubMed:18037411}.
-!- TISSUE SPECIFICITY: 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, PubMed:28745435). {ECO:0000269|PubMed:10517638,
ECO:0000269|PubMed:11553327, ECO:0000269|PubMed:12411744,
ECO:0000269|PubMed:15563610, ECO:0000269|PubMed:16481400,
ECO:0000269|PubMed:16943275, ECO:0000269|PubMed:26150102,
ECO:0000269|PubMed:28745435}.
-!- DEVELOPMENTAL STAGE: First expressed during L4 and peaks in the
adult male. {ECO:0000269|PubMed:12411744}.
-!- DOMAIN: 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.
{ECO:0000269|PubMed:18037411}.
-!- PTM: Phosphorylated. CK2 (kin-3 and kin-10) and calcineurin act
antagonistically to regulate the phosphorylation state.
{ECO:0000269|PubMed:16481400}.
-!- DISRUPTION PHENOTYPE: Worms exhibit defects in 2 aspects of male
mating behavior: response to hermaphrodite contact and vulva
location. {ECO:0000269|PubMed:11553327,
ECO:0000269|PubMed:28745435}.
-!- SIMILARITY: Belongs to the polycystin family. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; AL132862; CAB60565.3; -; Genomic_DNA.
RefSeq; NP_502838.3; NM_070437.4.
UniGene; Cel.12535; -.
ProteinModelPortal; Q9U1S7; -.
IntAct; Q9U1S7; 4.
MINT; MINT-3385171; -.
STRING; 6239.Y73F8A.1; -.
TCDB; 1.A.5.2.4; the polycystin cation channel (pcc) family.
iPTMnet; Q9U1S7; -.
PaxDb; Q9U1S7; -.
PeptideAtlas; Q9U1S7; -.
EnsemblMetazoa; Y73F8A.1; Y73F8A.1; WBGene00004035.
GeneID; 178424; -.
KEGG; cel:CELE_Y73F8A.1; -.
UCSC; Y73F8A.1; c. elegans.
CTD; 178424; -.
WormBase; Y73F8A.1; CE38663; WBGene00004035; pkd-2.
eggNOG; KOG3599; Eukaryota.
eggNOG; ENOG410XTGE; LUCA.
GeneTree; ENSGT00700000104221; -.
HOGENOM; HOG000230858; -.
InParanoid; Q9U1S7; -.
KO; K04986; -.
OMA; FSTFVKC; -.
OrthoDB; EOG091G034F; -.
PhylomeDB; Q9U1S7; -.
PRO; PR:Q9U1S7; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00004035; -.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
GO; GO:0005929; C:cilium; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:WormBase.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
GO; GO:0031090; C:organelle membrane; IDA:WormBase.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0071683; C:sensory dendrite; IDA:UniProtKB.
GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
GO; GO:0060179; P:male mating behavior; IDA:UniProtKB.
GO; GO:0007617; P:mating behavior; IMP:WormBase.
GO; GO:0023041; P:neuronal signal transduction; IC:WormBase.
GO; GO:0034606; P:response to hermaphrodite contact; IMP:UniProtKB.
GO; GO:0034608; P:vulval location; IMP:UniProtKB.
InterPro; IPR013122; PKD1_2_channel.
InterPro; IPR003915; PKD_2.
Pfam; PF08016; PKD_channel; 1.
PRINTS; PR01433; POLYCYSTIN2.
1: Evidence at protein level;
Behavior; Cell membrane; Cell projection; Cilium; Coiled coil;
Complete proteome; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport;
Zinc.
CHAIN 1 716 Polycystin-2.
/FTId=PRO_0000347285.
TOPO_DOM 1 72 Cytoplasmic. {ECO:0000255}.
TRANSMEM 73 93 Helical. {ECO:0000255}.
TOPO_DOM 94 324 Extracellular. {ECO:0000255}.
TRANSMEM 325 345 Helical. {ECO:0000255}.
TOPO_DOM 346 355 Cytoplasmic. {ECO:0000255}.
TRANSMEM 356 376 Helical. {ECO:0000255}.
TOPO_DOM 377 409 Extracellular. {ECO:0000255}.
TRANSMEM 410 430 Helical. {ECO:0000255}.
TOPO_DOM 431 447 Cytoplasmic. {ECO:0000255}.
TRANSMEM 448 468 Helical. {ECO:0000255}.
TOPO_DOM 469 482 Extracellular. {ECO:0000255}.
INTRAMEM 483 497 Pore-forming.
{ECO:0000250|UniProtKB:Q13563}.
TOPO_DOM 498 510 Extracellular. {ECO:0000255}.
TRANSMEM 511 531 Helical. {ECO:0000255}.
TOPO_DOM 532 716 Cytoplasmic. {ECO:0000255}.
COILED 613 680 {ECO:0000255}.
COMPBIAS 451 527 Phe-rich. {ECO:0000255}.
MOD_RES 534 534 Phosphoserine; by CK2.
{ECO:0000269|PubMed:16481400}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 377 377 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 496 496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 180 193 {ECO:0000250|UniProtKB:Q13563}.
MUTAGEN 534 534 S->A: Fails to rescue pkd-2 defects.
Prevents phosphorylation at this site.
{ECO:0000269|PubMed:16481400,
ECO:0000269|PubMed:17581863}.
MUTAGEN 534 534 S->D: Phospho-mimetic. Acts as if
constitutively phosphorylated.
{ECO:0000269|PubMed:16481400,
ECO:0000269|PubMed:17581863,
ECO:0000269|PubMed:26150102}.
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


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