O35245 (PKD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polycystin-2

Alternative name(s):
Polycystic kidney disease 2 protein homolog

Gene names

Name:

Pkd2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	966 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity. 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. Functions as a calcium permeable cation channel. Ref.7 Ref.10
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. Ref.3 Ref.8 Ref.11
Subcellular location	Membrane; Multi-pass membrane protein Potential. Endoplasmic reticulum By similarity. Cell projection › cilium Ref.7.
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
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 process	Ion transport Transport
Cellular component	Cell projection Cilium Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Ion channel
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade Inferred from direct assay PubMed 12007403. Source: MGI aorta development Inferred from electronic annotation. Source: Compara branching involved in ureteric bud morphogenesis Inferred from electronic annotation. Source: Compara cell cycle arrest Inferred from direct assay PubMed 12007403. 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: Compara cellular response to osmotic stress Inferred from electronic annotation. Source: Compara cytoplasmic sequestering of transcription factor Inferred from electronic annotation. Source: Compara detection of mechanical stimulus Inferred from mutant phenotype Ref.7. Source: MGI detection of nodal flow Inferred from mutant phenotype PubMed 21307093. Source: BHF-UCL determination of heart left/right asymmetry Inferred from electronic annotation. Source: Compara embryonic placenta development Inferred from mutant phenotype PubMed 20862291. Source: BHF-UCL heart development Inferred from mutant phenotype PubMed 10615132. Source: MGI 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: Compara metanephric S-shaped body morphogenesis Inferred from electronic annotation. Source: Compara metanephric ascending thin limb development Inferred from electronic annotation. Source: Compara metanephric cortex development Inferred from electronic annotation. Source: Compara metanephric cortical collecting duct development Inferred from electronic annotation. Source: Compara metanephric distal tubule development Inferred from electronic annotation. Source: Compara metanephric mesenchyme development Inferred from electronic annotation. Source: Compara metanephric part of ureteric bud development Inferred from electronic annotation. Source: Compara metanephric smooth muscle tissue development Inferred from electronic annotation. Source: Compara negative regulation of G1/S transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara 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: Compara placenta blood vessel development Inferred from mutant phenotype PubMed 20862291. Source: BHF-UCL positive regulation of cell cycle arrest Inferred from electronic annotation. Source: Compara positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S Inferred from electronic annotation. Source: Compara 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: Compara 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: Compara regulation of cAMP metabolic process Inferred from mutant phenotype PubMed 15790956. Source: MGI regulation of calcium ion import Inferred from electronic annotation. Source: Compara regulation of cell proliferation Inferred from electronic annotation. Source: Compara release of sequestered calcium ion into cytosol Inferred from mutant phenotype PubMed 19265036. Source: BHF-UCL renal artery morphogenesis Inferred from electronic annotation. Source: Compara renal tubule morphogenesis Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB spinal cord development Inferred from electronic annotation. Source: Compara
Cellular_component	basal cortex Inferred from direct assay PubMed 10770959. Source: BHF-UCL basal plasma membrane Inferred from electronic annotation. Source: Compara endoplasmic reticulum Inferred from direct assay Ref.3. Source: MGI filamentous actin Inferred from electronic annotation. Source: Compara integral to cytosolic side of endoplasmic reticulum membrane Inferred from electronic annotation. Source: Compara integral to lumenal side of endoplasmic reticulum membrane Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from electronic annotation. Source: Compara lamellipodium Inferred from electronic annotation. Source: Compara microtubule basal body Inferred from sequence orthology PubMed 15337773. Source: MGI 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_function	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: Compara potassium channel activity Inferred from direct assay PubMed 12640140. Source: MGI voltage-gated calcium channel activity Inferred from electronic annotation. Source: Compara voltage-gated sodium channel activity Inferred from electronic annotation. Source: Compara
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 966	966	Polycystin-2		PRO_0000164357
Regions
	Topological domain	1 – 221	221	Cytoplasmic Potential
	Transmembrane	222 – 242	21	Helical; Potential
	Topological domain	243 – 466	224	Extracellular Potential
	Transmembrane	467 – 487	21	Helical; Potential
	Topological domain	488 – 503	16	Cytoplasmic Potential
	Transmembrane	504 – 524	21	Helical; Potential
	Topological domain	525 – 548	24	Extracellular Potential
	Transmembrane	549 – 569	21	Helical; Potential
	Topological domain	570 – 596	27	Cytoplasmic Potential
	Transmembrane	597 – 617	21	Helical; Potential
	Topological domain	618 – 656	39	Extracellular Potential
	Transmembrane	657 – 677	21	Helical; Potential
	Topological domain	678 – 966	289	Cytoplasmic Potential
	Domain	748 – 783	36	EF-hand
	Calcium binding	761 – 772	12	By similarity
	Region	702 – 792	91	EF-hand domain By similarity
	Region	801 – 820	20	Linker By similarity
	Region	821 – 966	146	C-terminal coiled coil domain By similarity
	Coiled coil	837 – 917	81	Potential
	Motif	314 – 326	13	Polycystin motif
	Compositional bias	95 – 99	5	Poly-Asp
	Compositional bias	151 – 154	4	Poly-Arg
Amino acid modifications
	Modified residue	810	1	Phosphoserine Ref.9
	Glycosylation	297	1	N-linked (GlcNAc...) Potential
	Glycosylation	303	1	N-linked (GlcNAc...) Potential
	Glycosylation	326	1	N-linked (GlcNAc...) Potential
	Glycosylation	360	1	N-linked (GlcNAc...) Potential
	Glycosylation	373	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	474 – 481	8	CEIIFCFF → FICSSYGD in isoform 2.		VSP_042485
	Alternative sequence	482 – 966	485	Missing in isoform 2.		VSP_042486
	Alternative sequence	515 – 570	56	Missing in isoform 3.		VSP_042487
	Alternative sequence	631 – 644	14	IFTQF…GDINF → IICSWRSSMIRTLK in isoform 4.		VSP_042488
	Alternative sequence	645 – 966	322	Missing in isoform 4.		VSP_042489
	Alternative sequence	746 – 839	94	Missing in isoform 5.		VSP_042490
Experimental info
	Sequence conflict	365	1	M → I in AAC53388. Ref.1
	Sequence conflict	370	1	K → R in AAC53388. Ref.1
	Sequence conflict	560	1	S → A in AAC53388. Ref.1
	Sequence conflict	688 – 689	2	DL → SV in CAA74551. Ref.2
	Sequence conflict	746	1	K → E in CAA73727. Ref.2
	Sequence conflict	746	1	K → E in CAA74551. Ref.2
	Sequence conflict	746	1	K → E in ACN11624. Ref.3
	Sequence conflict	800	1	S → N in BAC35407. Ref.4
	Sequence conflict	942	1	P → S in AAC53388. Ref.1
	Sequence conflict	957	1	G → S in AAC53388. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 59B96AB3AE5226D3	FASTA	966	108,982
	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
	Isoform 2 (delta6) [UniParc]. Checksum: FE3F3890EA24ED54	FASTA	481	53,299
	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 LAAFICSSYG D
	Isoform 3 (delta7) [UniParc]. Checksum: 0440C0F721450995	FASTA	910	102,420
	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 VIVVLFKFIN FNRTMSQLST TMSRCAKDLF 550 560 570 580 590 600 GFTIMFSIIF LAYAQLAYLV FGTQVDDFST FQECIFTQFR IILGDINFAE IEEANRVLGP 610 620 630 640 650 660 LYFTTFVFFM FFILLNMFLA IINDSYSEVK SDLAQQKAEM ELSDLIRKGC QKALVKLKLK 670 680 690 700 710 720 RNTVDAISES LRQGGGKLNF DELRQDLKGK GHTDAEIEAI FTKYDQDGDQ ELTEREHQQM 730 740 750 760 770 780 RDDLEKERED LDLEHSSLPR PMSSRSFPRS LDDSEEEDDE DSGHSSRRRG SISSGVSYEE 790 800 810 820 830 840 FQVLVRRVDR MEHSIGSIVS KIDAVIVKLE IMERAKLKRR EVLGRLLDGV AEDARLGRDS 850 860 870 880 890 900 EIHREQMERL VREELERWES DDAASQTGHG VSTQVGLGGQ PHPRNPRPPS SQSAEGLEGG 910 GGNGSANVHA
	Isoform 4 (delta9) [UniParc]. Checksum: 10DCCE0B2DD5C4AD	FASTA	644	72,702
	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 MFSIIFLAYA QLAYLVFGTQ VDDFSTFQEC IICSWRSSMI RTLK
	Isoform 5 (delta12/13) [UniParc]. Checksum: 855914112AD1FEB7	FASTA	872	98,082
	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 QDLKGLVRRV DRMEHSIGSI VSKIDAVIVK LEIMERAKLK 790 800 810 820 830 840 RREVLGRLLD GVAEDARLGR DSEIHREQME RLVREELERW ESDDAASQTG HGVSTQVGLG 850 860 870 GQPHPRNPRP PSSQSAEGLE GGGGNGSANV HA

References

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[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. , 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. , 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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, MASS SPECTROMETRY. Tissue: Melanoma.
[10]	"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.
[11]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF014010 mRNA. Translation: AAC53388.1. Y13278 mRNA. Translation: CAA73727.1. Y14105 , 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.
IPI	IPI00314352. IPI00986374.
RefSeq	NP_032887.3. NM_008861.3.
UniGene	Mm.483692. Mm.6442.
3D structure databases
ProteinModelPortal	O35245.
SMR	O35245. Positions 723-793, 832-868.
ModBase	Search...
PTM databases
PhosphoSite	O35245.
Proteomic databases
PaxDb	O35245.
PRIDE	O35245.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000086831; ENSMUSP00000084041; ENSMUSG00000034462.
GeneID	18764.
KEGG	mmu:18764.
UCSC	uc012eab.1. mouse. uc012eac.1. mouse.
Organism-specific databases
CTD	5311.
MGI	MGI:1099818. Pkd2.
Phylogenomic databases
eggNOG	NOG325704.
GeneTree	ENSGT00700000104221.
HOGENOM	HOG000230858.
HOVERGEN	HBG014945.
InParanoid	O35245.
KO	K04986.
OMA	AWSRDNP.
OrthoDB	EOG473PQQ.
Gene expression databases
Bgee	O35245.
CleanEx	MM_PKD2.
Genevestigator	O35245.
GermOnline	ENSMUSG00000034462. Mus musculus.
Family and domain databases
Gene3D	1.10.238.10. 1 hit. 1.20.120.350. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. IPR002048. EF_hand_dom. IPR027359. K_channel_four-helix_dom. IPR013122. PKD1_2_channel. IPR003915. PKD_2. [Graphical view]
Pfam	PF08016. PKD_channel. 1 hit. [Graphical view]
PRINTS	PR01433. POLYCYSTIN2.
PROSITE	PS00018. EF_HAND_1. False negative. PS50222. EF_HAND_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PKD2. mouse.
NextBio	294963.
SOURCE	Search...

Entry information

Entry name

PKD2_MOUSE

Accession

Primary (citable) accession number: O35245
Secondary accession number(s): C0KJK2 , 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:	May 29, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program