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Polycystic kidney disease 2-like 1 protein (Polycystin-2 homolog)

 PK2L1_MOUSE             Reviewed;         760 AA.
A2A259; Q14B55; Q14B73; Q80ZH4;
19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
25-OCT-2017, entry version 81.
RecName: Full=Polycystic kidney disease 2-like 1 protein;
AltName: Full=Polycystin-2 homolog;
Name=Pkd2l1; Synonyms=Trpp3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
INTERACTION WITH PKD1L3, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=16891422; DOI=10.1073/pnas.0602702103;
Ishimaru Y., Inada H., Kubota M., Zhuang H., Tominaga M.,
Matsunami H.;
"Transient receptor potential family members PKD1L3 and PKD2L1 form a
candidate sour taste receptor.";
Proc. Natl. Acad. Sci. U.S.A. 103:12569-12574(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Brain;
Guo L., Zhou J.;
"Cloning and gene targeting of murine Pkdl gene.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PKD1, AND MUTAGENESIS
OF LYS-568 AND ASP-576.
PubMed=15548533; DOI=10.1074/jbc.M411496200;
Murakami M., Ohba T., Xu F., Shida S., Satoh E., Ono K., Miyoshi I.,
Watanabe H., Ito H., Iijima T.;
"Genomic organization and functional analysis of murine PKD2L1.";
J. Biol. Chem. 280:5626-5635(2005).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16929298; DOI=10.1038/nature05084;
Huang A.L., Chen X., Hoon M.A., Chandrashekar J., Guo W., Trankner D.,
Ryba N.J., Zuker C.S.;
"The cells and logic for mammalian sour taste detection.";
Nature 442:934-938(2006).
[7]
TISSUE SPECIFICITY.
PubMed=18156604; DOI=10.1093/chemse/bjm083;
Kataoka S., Yang R., Ishimaru Y., Matsunami H., Sevigny J.,
Kinnamon J.C., Finger T.E.;
"The candidate sour taste receptor, PKD2L1, is expressed by type III
taste cells in the mouse.";
Chem. Senses 33:243-254(2008).
[8]
FUNCTION.
PubMed=19833970; DOI=10.1126/science.1174601;
Chandrashekar J., Yarmolinsky D., von Buchholtz L., Oka Y., Sly W.,
Ryba N.J., Zuker C.S.;
"The taste of carbonation.";
Science 326:443-445(2009).
[9]
ENZYME REGULATION.
PubMed=20406802; DOI=10.1074/jbc.C110.132944;
Kawaguchi H., Yamanaka A., Uchida K., Shibasaki K., Sokabe T.,
Maruyama Y., Yanagawa Y., Murakami S., Tominaga M.;
"Activation of polycystic kidney disease-2-like 1 (PKD2L1)-PKD1L3
complex by acid in mouse taste cells.";
J. Biol. Chem. 285:17277-17281(2010).
[10]
FUNCTION.
PubMed=21098668; DOI=10.1073/pnas.1013664107;
Chang R.B., Waters H., Liman E.R.;
"A proton current drives action potentials in genetically identified
sour taste cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:22320-22325(2010).
[11]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-523; ASP-525 AND ASP-530.
PubMed=21185261; DOI=10.1016/j.bbrc.2010.12.086;
Fujimoto C., Ishimaru Y., Katano Y., Misaka T., Yamasoba T.,
Asakura T., Abe K.;
"The single pore residue Asp523 in PKD2L1 determines Ca2+ permeation
of the PKD1L3/PKD2L1 complex.";
Biochem. Biophys. Res. Commun. 404:946-951(2011).
[12]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=21625513; DOI=10.1371/journal.pone.0020007;
Horio N., Yoshida R., Yasumatsu K., Yanagawa Y., Ishimaru Y.,
Matsunami H., Ninomiya Y.;
"Sour taste responses in mice lacking PKD channels.";
PLoS ONE 6:E20007-E20007(2011).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24336288; DOI=10.1038/nature12833;
Delling M., DeCaen P.G., Doerner J.F., Febvay S., Clapham D.E.;
"Primary cilia are specialized calcium signalling organelles.";
Nature 504:311-314(2013).
[14]
FUNCTION.
PubMed=24336289; DOI=10.1038/nature12832;
DeCaen P.G., Delling M., Vien T.N., Clapham D.E.;
"Direct recording and molecular identification of the calcium channel
of primary cilia.";
Nature 504:315-318(2013).
-!- FUNCTION: Pore-forming subunit of a ciliary calcium channel that
controls calcium concentration within primary cilia without
affecting cytoplasmic calcium concentration. Forms a heterodimer
with PKD1L1 in primary cilia and forms a calcium-permeant ciliary
channel that regulates sonic hedgehog/SHH signaling and GLI2
transcription. May act as a sour taste receptor by forming a
calcium channel with PKD1L3 in gustatory cells; however, its
contribution to sour taste perception is unclear in vivo and may
be indirect. May play a role in the perception of carbonation
taste. {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422,
ECO:0000269|PubMed:16929298, ECO:0000269|PubMed:19833970,
ECO:0000269|PubMed:21098668, ECO:0000269|PubMed:21625513,
ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289}.
-!- ENZYME REGULATION: The calcium channel is gated following an off-
response property by acid: gated open after the removal of acid
stimulus, but not during acid application.
{ECO:0000269|PubMed:20406802}.
-!- SUBUNIT: Homotrimer; trimerization is independent of calcium-
binding. Calcium channels are probably composed of 3 subunit of
PKD2L1 and 1 subunit of some PKD1 protein (PKD1, PKD1L1, PKD1L2 or
PKDL3). Interacts with PKD1L1; to form ciliary calcium channel.
Interacts with PKD1L3, to form putative sour taste receptor.
Interacts with PKD1. Interacts with RACK1; inhibits the channel
activity possibly by impairing localization to the cell membrane.
{ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15594711, EBI-15594711;
Q2EG98:Pkd1l3; NbExp=2; IntAct=EBI-15594711, EBI-15594779;
-!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
membrane; Multi-pass membrane protein. Endoplasmic reticulum.
Note=Interaction with PKD1 or PKD1L3 is required for localization
to the cell membrane.
-!- TISSUE SPECIFICITY: Expressed in all 4 taste areas in taste buds:
circumvallate papillae, foliate papillae, fungiform papillae and
palate. Expressed in cells distinct from those mediating sweet,
umami and bitter taste (at protein level). Expressed in type III
taste cells (at protein level). {ECO:0000269|PubMed:16891422,
ECO:0000269|PubMed:16929298, ECO:0000269|PubMed:18156604,
ECO:0000269|PubMed:21625513}.
-!- DOMAIN: The EF-hand domain probably mediates calcium-binding. It
is not required for channel activation (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Intestinal malrotation in 50% of animals,
while other organs do not show major organ laterality defects
Intestinal malformations are associated with SHH pathway defects
during early development (PubMed:24336288). Partial reduction of
chorda tympani nerve response to sour stimuli, without affecting
sweet, salty, bitter, and umami perception (PubMed:21625513).
{ECO:0000269|PubMed:21625513, ECO:0000269|PubMed:24336288}.
-!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
-!- CAUTION: Pkd1l3 and Pkd2l1 have been defined as sour taste
receptor in gustatory cells based on a number of indirect
evidences: Pkd2l1 is expressed in a subset of taste receptor cells
distinct from those responsible for sweet, bitter and unami taste
and genetic elimination of cells expressing Pkd2l1 reduces
gustatory nerve responses to sour taste stimuli (PubMed:16891422,
PubMed:16929298). However, a number of experiments have recently
shown that the sour taste receptor activity is probably indirect:
mice lacking Pkd2l1 only show partial defects in sour taste
perception (PubMed:21625513). Moreover, the PKD1L3-PKD2L1
heteromer, when expressed in cells does not respond to acid
stimuli used to evoke proton currents in taste cells
(PubMed:21098668). {ECO:0000305|PubMed:16891422,
ECO:0000305|PubMed:16929298, ECO:0000305|PubMed:21098668,
ECO:0000305|PubMed:21625513}.
-----------------------------------------------------------------------
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EMBL; AB290927; BAF45380.1; -; mRNA.
EMBL; AF271381; AAK58371.1; -; mRNA.
EMBL; AC125101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC116297; AAI16298.1; -; mRNA.
EMBL; BC116323; AAI16324.2; -; mRNA.
CCDS; CCDS29846.1; -.
RefSeq; NP_852087.2; NM_181422.3.
UniGene; Mm.308481; -.
ProteinModelPortal; A2A259; -.
SMR; A2A259; -.
BioGrid; 236700; 1.
DIP; DIP-61250N; -.
IntAct; A2A259; 1.
STRING; 10090.ENSMUSP00000045675; -.
TCDB; 1.A.5.2.2; the polycystin cation channel (pcc) family.
PhosphoSitePlus; A2A259; -.
PaxDb; A2A259; -.
PeptideAtlas; A2A259; -.
PRIDE; A2A259; -.
Ensembl; ENSMUST00000042026; ENSMUSP00000045675; ENSMUSG00000037578.
GeneID; 329064; -.
KEGG; mmu:329064; -.
UCSC; uc008hpm.2; mouse.
CTD; 9033; -.
MGI; MGI:1352448; Pkd2l1.
eggNOG; KOG3599; Eukaryota.
eggNOG; ENOG410XTGE; LUCA.
GeneTree; ENSGT00700000104221; -.
HOGENOM; HOG000230858; -.
HOVERGEN; HBG014945; -.
InParanoid; A2A259; -.
KO; K04990; -.
OMA; FSTFVKC; -.
OrthoDB; EOG091G034F; -.
PhylomeDB; A2A259; -.
TreeFam; TF316484; -.
PRO; PR:A2A259; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000037578; -.
Genevisible; A2A259; MM.
GO; GO:0034704; C:calcium channel complex; IMP:UniProtKB.
GO; GO:0034703; C:cation channel complex; IDA:BHF-UCL.
GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0097730; C:non-motile cilium; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IPI:MGI.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
GO; GO:0005227; F:calcium activated cation channel activity; ISO:MGI.
GO; GO:0005262; F:calcium channel activity; IMP:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0015269; F:calcium-activated potassium channel activity; ISO:MGI.
GO; GO:0005261; F:cation channel activity; IPI:MGI.
GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051371; F:muscle alpha-actinin binding; ISO:MGI.
GO; GO:0005272; F:sodium channel activity; ISO:MGI.
GO; GO:0006812; P:cation transport; IDA:BHF-UCL.
GO; GO:0071468; P:cellular response to acidic pH; IDA:BHF-UCL.
GO; GO:0001581; P:detection of chemical stimulus involved in sensory perception of sour taste; IDA:BHF-UCL.
GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
GO; GO:0050915; P:sensory perception of sour taste; ISO:MGI.
GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR013122; PKD1_2_channel.
InterPro; IPR003915; PKD_2.
Pfam; PF08016; PKD_channel; 1.
PRINTS; PR01433; POLYCYSTIN2.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS50222; EF_HAND_2; 1.
1: Evidence at protein level;
Calcium; Calcium channel; Calcium transport; Cell membrane;
Cell projection; Cilium; Coiled coil; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Ion channel;
Ion transport; Membrane; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 760 Polycystic kidney disease 2-like 1
protein.
/FTId=PRO_0000425551.
TOPO_DOM 1 103 Cytoplasmic. {ECO:0000255}.
TRANSMEM 104 124 Helical. {ECO:0000255}.
TOPO_DOM 125 313 Extracellular. {ECO:0000255}.
TRANSMEM 314 334 Helical. {ECO:0000255}.
TOPO_DOM 335 347 Cytoplasmic. {ECO:0000255}.
TRANSMEM 348 368 Helical. {ECO:0000255}.
TOPO_DOM 369 385 Extracellular. {ECO:0000255}.
TRANSMEM 386 406 Helical. {ECO:0000255}.
TOPO_DOM 407 476 Cytoplasmic. {ECO:0000255}.
TRANSMEM 477 497 Helical. {ECO:0000255}.
TOPO_DOM 498 511 Extracellular. {ECO:0000255}.
INTRAMEM 512 526 Pore-forming.
{ECO:0000250|UniProtKB:Q13563}.
TOPO_DOM 527 539 Extracellular. {ECO:0000255}.
TRANSMEM 540 560 Helical. {ECO:0000255}.
TOPO_DOM 561 760 Cytoplasmic. {ECO:0000255}.
DOMAIN 630 665 EF-hand. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 643 654 {ECO:0000255|PROSITE-ProRule:PRU00448}.
REGION 701 760 Required for protein homotrimerization.
{ECO:0000250}.
COILED 559 580 {ECO:0000255}.
COILED 650 682 {ECO:0000255}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 505 505 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 210 223 {ECO:0000250|UniProtKB:Q13563}.
MUTAGEN 523 523 D->E: Little or no effect on calcium
channel activity.
{ECO:0000269|PubMed:21185261}.
MUTAGEN 523 523 D->N: Impaired calcium channel activity.
{ECO:0000269|PubMed:21185261}.
MUTAGEN 525 525 D->N: Little or no effect on calcium
channel activity.
{ECO:0000269|PubMed:21185261}.
MUTAGEN 530 530 D->N: Little or no effect on calcium
channel activity.
{ECO:0000269|PubMed:21185261}.
MUTAGEN 568 568 K->A: Induces localization to the cell
surface when expressed in absence of
PKD1. {ECO:0000269|PubMed:15548533}.
MUTAGEN 576 576 D->A: Induces localization to the
endoplasmic reticulum when expressed in
absence of PKD1.
{ECO:0000269|PubMed:15548533}.
CONFLICT 114 114 I -> V (in Ref. 2; AAK58371 and 4;
AAI16324/AAI16298). {ECO:0000305}.
CONFLICT 202 203 QL -> HV (in Ref. 2; AAK58371).
{ECO:0000305}.
CONFLICT 438 438 Y -> D (in Ref. 2; AAK58371).
{ECO:0000305}.
CONFLICT 482 482 I -> V (in Ref. 2; AAK58371).
{ECO:0000305}.
CONFLICT 756 756 L -> P (in Ref. 4; AAI16324/AAI16298).
{ECO:0000305}.
SEQUENCE 760 AA; 87234 MW; 4C76777051CFC2EF CRC64;
MNSMESPKNQ ELQTLGNRAW DNPAYSDPPS PNRTLRICTV SSVALPETQP KKPEVRCQEK
TQRTLVSSCC LHICRSIRGL WGTTLTENTA ENRELYVKTT LRELVVYIVF LVDICLLTYG
MTSSSAYYYT KVMSELFLHT PSDSGVSFQT ISSMSDFWDF AQGPLLDSLY WTKWYNNQSL
GRGSHSFIYY ENLLLGAPRL RQLRVRNDSC VVHEDFREDI LNCYDVYSPD KEDQLPFGPQ
NGTAWTYHSQ NELGGSSHWG RLTSYSGGGY YLDLPGSRQA SAEALQGLQE GLWLDRGTRV
VFIDFSVYNA NINLFCILRL VVEFPATGGT IPSWQIRTVK LIRYVNNWDF FIVGCEVVFC
VFIFYYVVEE ILEIHLHRLR YLSSVWNILD LVVILLSIVA VGFHIFRTLE VNRLMGKLLQ
QPDTYADFEF LAFWQTQYNN MNAVNLFFAW IKIFKYISFN KTMTQLSSTL ARCAKDILGF
AIMFFIVFFA YAQLGYLLFG TQVENFSTFV KCIFTQFRII LGDFDYNAID NANRILGPVY
FVTYVFFVFF VLLNMFLAII NDTYSEVKEE LAGQKDQLQL SDFLKQSYNK TLLRLRLRKE
RVSDVQKVLK GGEPEIQFED FTSTLRELGH EEHEITAAFT RFDQDGDHIL DEEEQEQMRQ
GLEEERVTLN AEIENLGRSV GHSPPGELGA EAARGQSWVS GEEFDMLTRR VLQLQCVLEG
VVSQIDAVGS KLKMLERKGE LAPSPGMGEP AVWENLYNPS


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