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O35245 (PKD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polycystin-2
Alternative name(s):
Polycystic kidney disease 2 protein homolog
Gene names
Name:Pkd2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length966 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a calcium permeable cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. PKD1 and PKD2 may function through a common signaling pathway that is necessary for normal tubulogenesis. Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. Also involved in left/right axis specification downstream of nodal flow: forms a complex with PKD2 in cilia to facilitate flow detection in left/right patterning. Ref.7 Ref.9 Ref.11

Subunit structure

Forms homooligomers. Isoform 1 interacts with PKD1 while isoform 3 does not. PKD1 requires the presence of PKD2 for stable expression. Interacts with CD2AP. Interacts with HAX1 By similarity. Interacts with NEK8. Part of a complex containing AKAP5, ADCY5, ADCY6 and PDE4C. Isoform 3 does not interact with PKD1. Interacts with PKD1L1. Ref.3 Ref.8 Ref.10 Ref.11

Subcellular location

Cell projectioncilium membrane; Multi-pass membrane protein. Endoplasmic reticulum By similarity Ref.7 Ref.11.

Tissue specificity

Expressed in mesenchymally derived structures in the developing embryo at day 12.5. Isoform 1 is predominantly expressed in kidney at all developmental stages with high levels also detected in lung. Isoform 3 shows highest expression in brain with lower expression in kidney and lung, low levels in thymus and is hardly detectable in liver. Ref.2 Ref.3 Ref.11

Domain

The C-terminal coiled-coil domain binds calcium and undergoes a calcium-induced conformation change. It is implicated in oligomerization and the interaction with PKD1 By similarity.

Sequence similarities

Belongs to the polycystin family.

Contains 1 EF-hand domain.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell membrane
Cell projection
Cilium
Endoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionIon channel
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Inferred from direct assay PubMed 12007403. Source: MGI

aorta development

Inferred from electronic annotation. Source: Ensembl

branching involved in ureteric bud morphogenesis

Inferred from electronic annotation. Source: Ensembl

calcium ion transport

Inferred from mutant phenotype Ref.7. Source: MGI

cell cycle arrest

Inferred from direct assay PubMed 12007403. Source: MGI

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 12874107. Source: MGI

cellular response to fluid shear stress

Inferred from mutant phenotype PubMed 19265036. Source: BHF-UCL

cellular response to hydrostatic pressure

Inferred from electronic annotation. Source: Ensembl

cellular response to osmotic stress

Inferred from electronic annotation. Source: Ensembl

cytoplasmic sequestering of transcription factor

Inferred from electronic annotation. Source: Ensembl

detection of mechanical stimulus

Inferred from mutant phenotype Ref.7. Source: MGI

detection of nodal flow

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

determination of left/right symmetry

Inferred from mutant phenotype PubMed 12062060. Source: MGI

determination of liver left/right asymmetry

Inferred from electronic annotation. Source: Ensembl

embryonic placenta development

Inferred from mutant phenotype PubMed 20862291. Source: BHF-UCL

heart development

Inferred from mutant phenotype PubMed 10615132. Source: MGI

heart looping

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from mutant phenotype PubMed 10615132. Source: MGI

liver development

Inferred from genetic interaction PubMed 21685914. Source: MGI

mesonephric duct development

Inferred from electronic annotation. Source: Ensembl

metanephric S-shaped body morphogenesis

Inferred from electronic annotation. Source: Ensembl

metanephric ascending thin limb development

Inferred from electronic annotation. Source: Ensembl

metanephric cortex development

Inferred from electronic annotation. Source: Ensembl

metanephric cortical collecting duct development

Inferred from electronic annotation. Source: Ensembl

metanephric distal tubule development

Inferred from electronic annotation. Source: Ensembl

metanephric mesenchyme development

Inferred from electronic annotation. Source: Ensembl

metanephric part of ureteric bud development

Inferred from electronic annotation. Source: Ensembl

metanephric smooth muscle tissue development

Inferred from electronic annotation. Source: Ensembl

negative regulation of G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

negative regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 17404231. Source: MGI

neural tube development

Inferred from electronic annotation. Source: Ensembl

placenta blood vessel development

Inferred from mutant phenotype PubMed 20862291. Source: BHF-UCL

positive regulation of cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB

positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from mutant phenotype PubMed 19265036. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

potassium ion transmembrane transport

Inferred from direct assay PubMed 12640140. Source: GOC

regulation of cAMP metabolic process

Inferred from mutant phenotype PubMed 15790956. Source: MGI

regulation of calcium ion import

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

release of sequestered calcium ion into cytosol

Inferred from mutant phenotype PubMed 19265036. Source: BHF-UCL

renal artery morphogenesis

Inferred from electronic annotation. Source: Ensembl

renal system development

Inferred from genetic interaction PubMed 21685914. Source: MGI

renal tubule morphogenesis

Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB

spinal cord development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasal cortex

Inferred from direct assay PubMed 10770959. Source: BHF-UCL

basal plasma membrane

Inferred from electronic annotation. Source: Ensembl

ciliary basal body

Inferred from direct assay PubMed 22031837. Source: MGI

ciliary membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cilium

Inferred from direct assay PubMed 19265036. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 10770959. Source: BHF-UCL

endoplasmic reticulum

Inferred from direct assay Ref.3. Source: MGI

filamentous actin

Inferred from electronic annotation. Source: Ensembl

integral component of cytoplasmic side of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

integral component of lumenal side of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: Ensembl

mitotic spindle

Inferred from direct assay PubMed 15123714. Source: BHF-UCL

motile primary cilium

Inferred from direct assay PubMed 15858826. Source: MGI

nonmotile primary cilium

Inferred from direct assay PubMed 12062067. Source: MGI

plasma membrane

Inferred from direct assay PubMed 12640140. Source: MGI

polycystin complex

Inferred from direct assay PubMed 11901144. Source: MGI

   Molecular_functionATPase binding

Inferred from physical interaction PubMed 18178578. Source: MGI

calcium channel activity

Inferred from direct assay PubMed 12640140. Source: MGI

calcium ion binding

Inferred from direct assay PubMed 20408813. Source: BHF-UCL

calcium-induced calcium release activity

Inferred from electronic annotation. Source: Ensembl

channel activity

Inferred from mutant phenotype PubMed 18235088. Source: MGI

identical protein binding

Inferred from physical interaction PubMed 20408813. Source: BHF-UCL

potassium channel activity

Inferred from direct assay PubMed 12640140. Source: MGI

receptor binding

Inferred from physical interaction PubMed 17404231. Source: MGI

voltage-gated calcium channel activity

Inferred from electronic annotation. Source: Ensembl

voltage-gated sodium channel activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O35245-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O35245-2)

Also known as: delta6;

The sequence of this isoform differs from the canonical sequence as follows:
     474-481: CEIIFCFF → FICSSYGD
     482-966: Missing.
Isoform 3 (identifier: O35245-3)

Also known as: delta7;

The sequence of this isoform differs from the canonical sequence as follows:
     515-570: Missing.
Isoform 4 (identifier: O35245-4)

Also known as: delta9;

The sequence of this isoform differs from the canonical sequence as follows:
     631-644: IFTQFRIILGDINF → IICSWRSSMIRTLK
     645-966: Missing.
Isoform 5 (identifier: O35245-5)

Also known as: delta12/13;

The sequence of this isoform differs from the canonical sequence as follows:
     746-839: Missing.
Note: Minor isoform.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 966966Polycystin-2
PRO_0000164357

Regions

Topological domain1 – 221221Cytoplasmic Potential
Transmembrane222 – 24221Helical; Potential
Topological domain243 – 466224Extracellular Potential
Transmembrane467 – 48721Helical; Potential
Topological domain488 – 50316Cytoplasmic Potential
Transmembrane504 – 52421Helical; Potential
Topological domain525 – 54824Extracellular Potential
Transmembrane549 – 56921Helical; Potential
Topological domain570 – 59627Cytoplasmic Potential
Transmembrane597 – 61721Helical; Potential
Topological domain618 – 65639Extracellular Potential
Transmembrane657 – 67721Helical; Potential
Topological domain678 – 966289Cytoplasmic Potential
Domain748 – 78336EF-hand
Calcium binding761 – 77212 By similarity
Region702 – 79291EF-hand domain By similarity
Region801 – 82020Linker By similarity
Region821 – 966146C-terminal coiled coil domain By similarity
Coiled coil837 – 91781 Potential
Motif314 – 32613Polycystin motif
Compositional bias95 – 995Poly-Asp
Compositional bias151 – 1544Poly-Arg

Amino acid modifications

Modified residue8101Phosphoserine By similarity
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation3261N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Potential
Glycosylation3731N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence474 – 4818CEIIFCFF → FICSSYGD in isoform 2.
VSP_042485
Alternative sequence482 – 966485Missing in isoform 2.
VSP_042486
Alternative sequence515 – 57056Missing in isoform 3.
VSP_042487
Alternative sequence631 – 64414IFTQF…GDINF → IICSWRSSMIRTLK in isoform 4.
VSP_042488
Alternative sequence645 – 966322Missing in isoform 4.
VSP_042489
Alternative sequence746 – 83994Missing in isoform 5.
VSP_042490

Experimental info

Mutagenesis4421E → G in lrm4; mice exhibit gross left-right abnormalities. Embryos do not show defects in kidney development. The nodes appear normal. Ref.11
Sequence conflict3651M → I in AAC53388. Ref.1
Sequence conflict3701K → R in AAC53388. Ref.1
Sequence conflict5601S → A in AAC53388. Ref.1
Sequence conflict688 – 6892DL → SV in CAA74551. Ref.2
Sequence conflict7461K → E in CAA73727. Ref.2
Sequence conflict7461K → E in CAA74551. Ref.2
Sequence conflict7461K → E in ACN11624. Ref.3
Sequence conflict8001S → N in BAC35407. Ref.4
Sequence conflict9421P → S in AAC53388. Ref.1
Sequence conflict9571G → S in AAC53388. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 59B96AB3AE5226D3

FASTA966108,982
        10         20         30         40         50         60 
MVNSRRVQPQ PPGDAGRSPA PRASGPGRLV AGGAGLAVPG GLGEQRGLEI EMERIRQAAA 

        70         80         90        100        110        120 
RDPPAGASAS PSPPLSSCSR QAWSRDNPGF EAEEDDDDDE VEGEEGGMVV EMDVEWRPGS 

       130        140        150        160        170        180 
RRSASSSAVS SVGARGRGLG SYRGAAHLSG RRRRLEDQGA QCPSPAGGGD PLHRHLPLEG 

       190        200        210        220        230        240 
QPPRVAWAER LVRGLRGLWG TRLMEESNAN REKYLKSVLR ELVTYLFFLV VLCILTYGMM 

       250        260        270        280        290        300 
SSNVYYYTRT LSQLFIDTPV SKTEKTNFKT LSSMEDFWKF TEGSFLDGLY WKAQTSNHTQ 

       310        320        330        340        350        360 
ADNRSFIFYE NLLLGVPRLR QLRVRNGSCS IPQDLRDEIK ECYDVYSVSS EDRAPFGPRN 

       370        380        390        400        410        420 
GTAWMYTSEK ELNGSSHWGI IASYSGAGYY LDLSRTREET AAQLAGLRRN FWLDRGTRAA 

       430        440        450        460        470        480 
FIDFSVYNAN INLFCVVRLL AEFPATGGVV PSWQFQPVKL IRYVTAFDFF LAACEIIFCF 

       490        500        510        520        530        540 
FIIYYVVEEI LEIRIHRLSY FRSFWNCLDV VIVVLSVVAM VINIYRMSNA EGLLQFLEDQ 

       550        560        570        580        590        600 
NSFPNFEHVA YWQIQFNNIS AVMVFLVWIK LFKFINFNRT MSQLSTTMSR CAKDLFGFTI 

       610        620        630        640        650        660 
MFSIIFLAYA QLAYLVFGTQ VDDFSTFQEC IFTQFRIILG DINFAEIEEA NRVLGPLYFT 

       670        680        690        700        710        720 
TFVFFMFFIL LNMFLAIIND SYSEVKSDLA QQKAEMELSD LIRKGCQKAL VKLKLKRNTV 

       730        740        750        760        770        780 
DAISESLRQG GGKLNFDELR QDLKGKGHTD AEIEAIFTKY DQDGDQELTE REHQQMRDDL 

       790        800        810        820        830        840 
EKEREDLDLE HSSLPRPMSS RSFPRSLDDS EEEDDEDSGH SSRRRGSISS GVSYEEFQVL 

       850        860        870        880        890        900 
VRRVDRMEHS IGSIVSKIDA VIVKLEIMER AKLKRREVLG RLLDGVAEDA RLGRDSEIHR 

       910        920        930        940        950        960 
EQMERLVREE LERWESDDAA SQTGHGVSTQ VGLGGQPHPR NPRPPSSQSA EGLEGGGGNG 


SANVHA 

« Hide

Isoform 2 (delta6) [UniParc].

Checksum: FE3F3890EA24ED54
Show »

FASTA48153,299
Isoform 3 (delta7) [UniParc].

Checksum: 0440C0F721450995
Show »

FASTA910102,420
Isoform 4 (delta9) [UniParc].

Checksum: 10DCCE0B2DD5C4AD
Show »

FASTA64472,702
Isoform 5 (delta12/13) [UniParc].

Checksum: 855914112AD1FEB7
Show »

FASTA87298,082

References

« Hide 'large scale' references
[1]"Molecular cloning, cDNA sequence analysis, and chromosomal localization of mouse Pkd2."
Wu G.Q., Mochizuki T., Le T.C., Cai Y., Hayashi T., Reynolds D.M., Somlo S.
Genomics 45:220-223(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Characterization of the murine polycystic kidney disease (Pkd2) gene."
Pennekamp P., Bogdanova N., Wilda M., Markoff A., Hameister H., Horst J., Dworniczak B.
Mamm. Genome 9:749-752(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]"A splice form of polycystin-2, lacking exon 7, does not interact with polycystin-1."
Hackmann K., Markoff A., Qian F., Bogdanova N., Germino G.G., Pennekamp P., Dworniczak B., Horst J., Gerke V.
Hum. Mol. Genet. 14:3249-3262(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORMS 2; 3; 4 AND 5), LACK OF INTERACTION OF ISOFORM 3 WITH PKD1, TISSUE SPECIFICITY.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Eye.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]"Cloning and characterization of the murine pkd2 promoter."
Park J.H., Li L., Cai Y., Hayashi T., Dong F., Maeda Y., Rubin C., Somlo S., Wu G.
Genomics 66:305-312(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-95.
Strain: 129/Ola.
[7]"Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells."
Nauli S.M., Alenghat F.J., Luo Y., Williams E., Vassilev P., Li X., Elia A.E., Lu W., Brown E.M., Quinn S.J., Ingber D.E., Zhou J.
Nat. Genet. 33:129-137(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Nek8 regulates the expression and localization of polycystin-1 and polycystin-2."
Sohara E., Luo Y., Zhang J., Manning D.K., Beier D.R., Zhou J.
J. Am. Soc. Nephrol. 19:469-476(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEK8.
[9]"Identification of signaling pathways regulating primary cilium length and flow-mediated adaptation."
Besschetnova T.Y., Kolpakova-Hart E., Guan Y., Zhou J., Olsen B.R., Shah J.V.
Curr. Biol. 20:182-187(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS REGULATOR OF CILIUM LENGTH.
[10]"Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases."
Choi Y.H., Suzuki A., Hajarnis S., Ma Z., Chapin H.C., Caplan M.J., Pontoglio M., Somlo S., Igarashi P.
Proc. Natl. Acad. Sci. U.S.A. 108:10679-10684(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AKAP5; ADCY5; ADCY6 AND PDE4C.
[11]"Pkd1l1 establishes left-right asymmetry and physically interacts with Pkd2."
Field S., Riley K.L., Grimes D.T., Hilton H., Simon M., Powles-Glover N., Siggers P., Bogani D., Greenfield A., Norris D.P.
Development 138:1131-1142(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PKD1L1, MUTAGENESIS OF GLU-442, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF014010 mRNA. Translation: AAC53388.1.
Y13278 mRNA. Translation: CAA73727.1.
Y14105 expand/collapse EMBL AC list , Y14106, Y14107, Y14108, Y14109, Y14110, Y14111, Y14112, Y14113, Y14114, Y14115, Y14116, Y14117, Y14118, Y14119 Genomic DNA. Translation: CAA74551.1.
Y14120 mRNA. Translation: CAA74552.1.
FJ609779 mRNA. Translation: ACN11624.1.
AK053502 mRNA. Translation: BAC35407.1.
AC123687 Genomic DNA. No translation available.
AC124106 Genomic DNA. No translation available.
AF242389 Genomic DNA. Translation: AAG13267.1.
RefSeqNP_032887.3. NM_008861.3.
XP_006534878.1. XM_006534815.1.
UniGeneMm.483692.
Mm.6442.

3D structure databases

ProteinModelPortalO35245.
SMRO35245. Positions 723-793, 832-868.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202205. 8 interactions.

PTM databases

PhosphoSiteO35245.

Proteomic databases

PaxDbO35245.
PRIDEO35245.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000086831; ENSMUSP00000084041; ENSMUSG00000034462. [O35245-1]
GeneID18764.
KEGGmmu:18764.
UCSCuc012eab.1. mouse. [O35245-1]
uc012eac.1. mouse. [O35245-3]

Organism-specific databases

CTD5311.
MGIMGI:1099818. Pkd2.

Phylogenomic databases

eggNOGNOG325704.
GeneTreeENSGT00700000104221.
HOGENOMHOG000230858.
HOVERGENHBG014945.
InParanoidO35245.
KOK04986.
OMAAWSRDNP.
OrthoDBEOG7N8ZTW.
TreeFamTF316484.

Gene expression databases

BgeeO35245.
CleanExMM_PKD2.
GenevestigatorO35245.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.20.120.350. 1 hit.
InterProIPR027359. Channel_four-helix_dom.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR013122. PKD1_2_channel.
IPR003915. PKD_2.
[Graphical view]
PfamPF08016. PKD_channel. 1 hit.
[Graphical view]
PRINTSPR01433. POLYCYSTIN2.
PROSITEPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPKD2. mouse.
NextBio294963.
PROO35245.
SOURCESearch...

Entry information

Entry namePKD2_MOUSE
AccessionPrimary (citable) accession number: O35245
Secondary accession number(s): C0KJK2 expand/collapse secondary AC list , E9Q4F6, E9QQA3, Q8BPR6, Q9ES37, Q9QWP0, Q9Z193, Q9Z194
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot