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Protein

Polycystin-2

Gene

Pkd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:12514735, PubMed:18695040, PubMed:27760766). Functions as outward-rectifying K+ channel, but is also permeable to Ca2+, and to a much lesser degree also to Na+ (PubMed:27760766). May contribute to the release of Ca2+ stores from the endoplasmic reticulum (By similarity). Together with TRPV4, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells (PubMed:9568711, PubMed:10615132). 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 (PubMed:20096584). Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning (PubMed:21307093, PubMed:22983710). Detection of asymmetric nodal flow gives rise to a Ca2+ signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality (PubMed:12062060, PubMed:21307093, PubMed:22983710).By similarity2 Publications7 Publications

Enzyme regulationi

Channnel activity is regulated by phosphorylation (By similarity). The channel is activated by increased cytoplasmic Ca2+ (in the µM range) and by membrane depolarization (PubMed:27760766).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi761CalciumBy similarity1
Metal bindingi763CalciumBy similarity1
Metal bindingi765CalciumBy similarity1
Metal bindingi767Calcium; via carbonyl oxygenBy similarity1
Metal bindingi772CalciumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi761 – 772PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • actinin binding Source: MGI
  • ATPase binding Source: MGI
  • calcium channel activity Source: MGI
  • calcium-induced calcium release activity Source: MGI
  • calcium ion binding Source: BHF-UCL
  • channel activity Source: MGI
  • cytoskeletal protein binding Source: MGI
  • HLH domain binding Source: MGI
  • identical protein binding Source: BHF-UCL
  • ion channel binding Source: MGI
  • muscle alpha-actinin binding Source: Ensembl
  • outward rectifier potassium channel activity Source: UniProtKB
  • phosphoprotein binding Source: MGI
  • potassium channel activity Source: MGI
  • protein homodimerization activity Source: MGI
  • receptor binding Source: MGI
  • voltage-gated calcium channel activity Source: MGI
  • voltage-gated cation channel activity Source: MGI
  • voltage-gated ion channel activity Source: MGI
  • voltage-gated potassium channel activity Source: MGI
  • voltage-gated sodium channel activity Source: MGI

GO - Biological processi

  • aorta development Source: Ensembl
  • branching involved in ureteric bud morphogenesis Source: Ensembl
  • calcium ion transmembrane transport Source: UniProtKB
  • calcium ion transport Source: MGI
  • cell cycle arrest Source: MGI
  • cellular calcium ion homeostasis Source: MGI
  • cellular response to calcium ion Source: UniProtKB
  • cellular response to cAMP Source: MGI
  • cellular response to fluid shear stress Source: BHF-UCL
  • cellular response to hydrostatic pressure Source: MGI
  • cellular response to osmotic stress Source: MGI
  • cytoplasmic sequestering of transcription factor Source: MGI
  • detection of mechanical stimulus Source: MGI
  • detection of nodal flow Source: BHF-UCL
  • determination of left/right symmetry Source: MGI
  • determination of liver left/right asymmetry Source: MGI
  • embryonic placenta development Source: BHF-UCL
  • heart development Source: MGI
  • heart looping Source: MGI
  • JAK-STAT cascade Source: MGI
  • kidney development Source: MGI
  • liver development Source: MGI
  • mesonephric duct development Source: Ensembl
  • metanephric ascending thin limb development Source: Ensembl
  • metanephric cortex development Source: Ensembl
  • metanephric cortical collecting duct development Source: Ensembl
  • metanephric distal tubule development Source: Ensembl
  • metanephric mesenchyme development Source: Ensembl
  • metanephric part of ureteric bud development Source: Ensembl
  • metanephric smooth muscle tissue development Source: Ensembl
  • metanephric S-shaped body morphogenesis Source: Ensembl
  • negative regulation of G1/S transition of mitotic cell cycle Source: MGI
  • negative regulation of ryanodine-sensitive calcium-release channel activity Source: MGI
  • neural tube development Source: Ensembl
  • placenta blood vessel development Source: BHF-UCL
  • positive regulation of cell cycle arrest Source: MGI
  • positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: MGI
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: MGI
  • positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • potassium ion transmembrane transport Source: UniProtKB
  • protein homotetramerization Source: MGI
  • regulation of calcium ion import Source: MGI
  • regulation of cAMP metabolic process Source: MGI
  • regulation of cell proliferation Source: MGI
  • release of sequestered calcium ion into cytosol Source: BHF-UCL
  • renal artery morphogenesis Source: Ensembl
  • renal system development Source: MGI
  • renal tubule morphogenesis Source: UniProtKB
  • sodium ion transmembrane transport Source: MGI
  • spinal cord development Source: Ensembl

Keywordsi

Molecular functionCalcium channel, Ion channel, Potassium channel, Voltage-gated channel
Biological processCalcium transport, Ion transport, Potassium transport, Transport
LigandCalcium, Metal-binding, Potassium

Names & Taxonomyi

Protein namesi
Recommended name:
Polycystin-2
Alternative name(s):
Polycystic kidney disease 2 protein homolog
Transient receptor potential cation channel subfamily P member 2Imported
Gene namesi
Name:Pkd2Imported
Synonyms:TRPP2Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1099818. Pkd2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 217CytoplasmicBy similarityAdd BLAST217
Transmembranei218 – 239Helical; Name=S1By similarityAdd BLAST22
Topological domaini240 – 466ExtracellularBy similarityAdd BLAST227
Transmembranei467 – 487Helical; Name=S2By similarityAdd BLAST21
Topological domaini488 – 503CytoplasmicBy similarityAdd BLAST16
Transmembranei504 – 524Helical; Name=S3By similarityAdd BLAST21
Topological domaini525 – 550ExtracellularBy similarityAdd BLAST26
Transmembranei551 – 571Helical; Name=S4By similarityAdd BLAST21
Topological domaini572 – 595CytoplasmicBy similarityAdd BLAST24
Transmembranei596 – 617Helical; Name=5By similarityAdd BLAST22
Topological domaini618 – 629ExtracellularBy similarityAdd BLAST12
Intramembranei630 – 644Pore-formingBy similarityAdd BLAST15
Topological domaini645 – 652ExtracellularBy similarity8
Transmembranei653 – 673Helical; Name=S6By similarityAdd BLAST21
Topological domaini674 – 966CytoplasmicBy similarityAdd BLAST293

GO - Cellular componenti

  • basal cortex Source: BHF-UCL
  • basal plasma membrane Source: MGI
  • ciliary basal body Source: MGI
  • ciliary membrane Source: UniProtKB
  • cilium Source: BHF-UCL
  • cytoplasm Source: BHF-UCL
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: MGI
  • endoplasmic reticulum membrane Source: MGI
  • extracellular exosome Source: MGI
  • filamentous actin Source: Ensembl
  • integral component of cytoplasmic side of endoplasmic reticulum membrane Source: MGI
  • integral component of lumenal side of endoplasmic reticulum membrane Source: MGI
  • integral component of plasma membrane Source: MGI
  • lamellipodium Source: MGI
  • mitotic spindle Source: BHF-UCL
  • motile cilium Source: MGI
  • non-motile cilium Source: MGI
  • plasma membrane Source: MGI
  • polycystin complex Source: MGI

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Complete embryonic lethality, with most embryos surviving up to about 16.5 dpc (PubMed:9568711, PubMed:10615132, PubMed:12062060). Embryos lacking Pkd2 develop normally up to 13.5 dpc, but after that about half of them display total body edema and focal hemorrhages (PubMed:10615132). Mutant embryos display defects in left-right laterality, including abnormal heart looping (PubMed:12062060). After 13.5 dpc, all embryos display defects in heart development, with defective formation of the interventricular septum (PubMed:10615132, PubMed:12062060). Besides, many display defective formation of the atrial septum and pericardial effusions (PubMed:10615132). After 14.5 dpc, the embyos display progressive cystic dilatation of pancreatic ducts (PubMed:10615132). After 15.5 dpc, they display progressive kidney cyst formation (PubMed:10615132). In contrast, liver development is normal, without any cyst formation (PubMed:10615132). Heterozygous mice with one null allele and one instable allele that leads to somatic loss of Pkd2 expression due to intragenic recombination all display bilateral renal cysts at an age of about 11 weeks (PubMed:9568711). These cysts cover 25-75% of the cut surface area of each kidney (PubMed:9568711). Progressive cyst formation leads eventually to renal failure and shortened lifespan (PubMed:10615132). Besides, these mice all display liver cysts and half of them display also bile duct proliferation (PubMed:9568711). About half of the heterozygous mice with one null allele and one instable allele that leads to somatic loss of Pkd2 expression due to intragenic recombination display visible pancreas cysts at an age of three months (PubMed:10615132). Mice homozygous for an instable allele that leads to somatic loss of Pkd2 expression due to intragenic recombination develop renal cysts that arise from cells that have lost Pkd2 expression (PubMed:9568711). Heterozygous mice that bear one null allele also have a reduced lifespan, but this is not due to kidney failure (PubMed:10615132).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi6R → G: No effect on location at nodal cilia and can rescue the laterality defect of null mutants. Abolishes location at nodal cilia and cannot complement the laterality defect of null mutants; when associated with DEL 819-966. 1 Publication1
Mutagenesisi442E → G in lrm4; mice exhibit gross left-right abnormalities. Embryos do not show defects in kidney development. The nodes appear normal. Abolishes location at nodal cilia, but does not affect interaction with Pkd1l1. 2 Publications1
Mutagenesisi509D → V: Abolishes location at nodal cilia and cannot complement the laterality defect of null mutants. 1 Publication1
Mutagenesisi819 – 966Missing : Abolishes location at nodal cilia and cannot complement the laterality defect of null mutants; when associated with G-6. 1 PublicationAdd BLAST148

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001643571 – 966Polycystin-2Add BLAST966

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei72PhosphoserineBy similarity1
Modified residuei76PhosphoserineBy similarity1
Modified residuei135Omega-N-methylarginineCombined sources1
Glycosylationi297N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi303N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi326N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi329 ↔ 342By similarity
Glycosylationi360N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi373N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei799PhosphoserineBy similarity1
Modified residuei806PhosphoserineCombined sources1
Modified residuei810PhosphoserineCombined sources1
Modified residuei827PhosphoserineCombined sources1

Post-translational modificationi

N-glycosylated (PubMed:11854751). The four subunits in a tetramer probably differ in the extent of glycosylation; simultaneous glycosylation of all experimentally validated sites would probably create steric hindrance (By similarity).By similarity1 Publication
Phosphorylated (PubMed:16551655). Phosphorylation is important for protein function; a mutant that lacks the N-terminal phosphorylation sites cannot complement a zebrafish pkd2-deficient mutant. PKD-mediated phosphorylation at the C-terminus regulates its function in the release of Ca2+ stores from the endoplasmic reticulum. PKA-mediated phosphorylation at a C-terminal site strongly increases the open probability of the channel, but does not increase single channel conductance.By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

MaxQBiO35245.
PaxDbiO35245.
PeptideAtlasiO35245.
PRIDEiO35245.

PTM databases

iPTMnetiO35245.
PhosphoSitePlusiO35245.

Expressioni

Tissue specificityi

Detected in kidney epithelium (at protein level) (PubMed:9568711, PubMed:10770959, PubMed:11854751). Highly expressed on basolateral membranes in distal convoluted tubules and medullary thick ascending limbs of Henle (PubMed:9568711). Detected at much lower levels in cortical and medullary collecting tubules, and not detected in the glomerular tuft, in thin limbs of Henle, interstitium and blood vessels (at protein level) (PubMed:9568711). 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.6 Publications

Developmental stagei

Ubiquitous in embryos at the early somite stage.1 Publication

Gene expression databases

BgeeiENSMUSG00000034462.
CleanExiMM_PKD2.
GenevisibleiO35245. MM.

Interactioni

Subunit structurei

Homotetramer. Interacts with PKD1, giving rise to a complex formed by one PKD1 chain and a PKD2 homooligomer. In vitro results suggest assembly of a complex composed of one PKD1 chain and a PKD2 trimer; the physiological significance of this is uncertain (By similarity). Isoform 1 interacts with PKD1 while isoform 3 does not (PubMed:16192288). Interacts with PKD1L1 (PubMed:21307093, PubMed:22983710). PKD1 requires the presence of PKD2 for stable expression (PubMed:16192288). Interacts with CD2AP (PubMed:10913159). Interacts with HAX1 (PubMed:10760273). Interacts with NEK8 (PubMed:18235101). Part of a complex containing AKAP5, ADCY5, ADCY6 and PDE4C (PubMed:21670265). Interacts (via C-terminus) with TRPV4 (via C-terminus) (PubMed:18695040). Interacts (via C-terminal acidic region) with PACS1 and PACS2; these interactions retain the protein in the endoplasmic reticulum and prevent trafficking to the cell membrane (PubMed:15692563).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Piezo1E2JF223EBI-9823400,EBI-9837938

GO - Molecular functioni

  • actinin binding Source: MGI
  • ATPase binding Source: MGI
  • cytoskeletal protein binding Source: MGI
  • HLH domain binding Source: MGI
  • identical protein binding Source: BHF-UCL
  • ion channel binding Source: MGI
  • muscle alpha-actinin binding Source: Ensembl
  • phosphoprotein binding Source: MGI
  • protein homodimerization activity Source: MGI
  • receptor binding Source: MGI

Protein-protein interaction databases

BioGridi202205. 11 interactors.
DIPiDIP-60904N.
IntActiO35245. 4 interactors.
STRINGi10090.ENSMUSP00000084041.

Structurei

3D structure databases

ProteinModelPortaliO35245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini748 – 783EF-handPROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni801 – 820LinkerBy similarityAdd BLAST20
Regioni808 – 819Important for interaction with PACS1 and PACS2By similarityAdd BLAST12

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili831 – 870By similarityAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi639 – 641Selectivity filterBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi95 – 99Poly-Asp5
Compositional biasi151 – 154Poly-Arg4

Domaini

The C-terminal coiled-coil domain is involved in oligomerization and the interaction with PKD1. The isolated coiled-coil domain forms a homotrimer in vitro; the homotrimer interacts with a single PKD1 chain. The coiled-coil domain binds calcium and undergoes a calcium-induced conformation change (in vitro).By similarity

Sequence similaritiesi

Belongs to the polycystin family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3599. Eukaryota.
ENOG410XTGE. LUCA.
GeneTreeiENSGT00700000104221.
HOGENOMiHOG000230858.
HOVERGENiHBG014945.
InParanoidiO35245.
KOiK04986.
OMAiQAWSRDN.
OrthoDBiEOG091G034F.
TreeFamiTF316484.

Family and domain databases

InterProiView protein in InterPro
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR013122. PKD1_2_channel.
IPR003915. PKD_2.
PfamiView protein in Pfam
PF08016. PKD_channel. 1 hit.
PRINTSiPR01433. POLYCYSTIN2.
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiView protein in PROSITE
PS50222. EF_HAND_2. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O35245-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVNSRRVQPQ PPGDAGRSPA PRASGPGRLV AGGAGLAVPG GLGEQRGLEI
60 70 80 90 100
EMERIRQAAA RDPPAGASAS PSPPLSSCSR QAWSRDNPGF EAEEDDDDDE
110 120 130 140 150
VEGEEGGMVV EMDVEWRPGS RRSASSSAVS SVGARGRGLG SYRGAAHLSG
160 170 180 190 200
RRRRLEDQGA QCPSPAGGGD PLHRHLPLEG QPPRVAWAER LVRGLRGLWG
210 220 230 240 250
TRLMEESNAN REKYLKSVLR ELVTYLFFLV VLCILTYGMM SSNVYYYTRT
260 270 280 290 300
LSQLFIDTPV SKTEKTNFKT LSSMEDFWKF TEGSFLDGLY WKAQTSNHTQ
310 320 330 340 350
ADNRSFIFYE NLLLGVPRLR QLRVRNGSCS IPQDLRDEIK ECYDVYSVSS
360 370 380 390 400
EDRAPFGPRN GTAWMYTSEK ELNGSSHWGI IASYSGAGYY LDLSRTREET
410 420 430 440 450
AAQLAGLRRN FWLDRGTRAA FIDFSVYNAN INLFCVVRLL AEFPATGGVV
460 470 480 490 500
PSWQFQPVKL IRYVTAFDFF LAACEIIFCF FIIYYVVEEI LEIRIHRLSY
510 520 530 540 550
FRSFWNCLDV VIVVLSVVAM VINIYRMSNA EGLLQFLEDQ NSFPNFEHVA
560 570 580 590 600
YWQIQFNNIS AVMVFLVWIK LFKFINFNRT MSQLSTTMSR CAKDLFGFTI
610 620 630 640 650
MFSIIFLAYA QLAYLVFGTQ VDDFSTFQEC IFTQFRIILG DINFAEIEEA
660 670 680 690 700
NRVLGPLYFT TFVFFMFFIL LNMFLAIIND SYSEVKSDLA QQKAEMELSD
710 720 730 740 750
LIRKGCQKAL VKLKLKRNTV DAISESLRQG GGKLNFDELR QDLKGKGHTD
760 770 780 790 800
AEIEAIFTKY DQDGDQELTE REHQQMRDDL EKEREDLDLE HSSLPRPMSS
810 820 830 840 850
RSFPRSLDDS EEEDDEDSGH SSRRRGSISS GVSYEEFQVL VRRVDRMEHS
860 870 880 890 900
IGSIVSKIDA VIVKLEIMER AKLKRREVLG RLLDGVAEDA RLGRDSEIHR
910 920 930 940 950
EQMERLVREE LERWESDDAA SQTGHGVSTQ VGLGGQPHPR NPRPPSSQSA
960
EGLEGGGGNG SANVHA
Length:966
Mass (Da):108,982
Last modified:July 27, 2011 - v2
Checksum:i59B96AB3AE5226D3
GO
Isoform 2 (identifier: O35245-2) [UniParc]FASTAAdd to basket
Also known as: delta6

The sequence of this isoform differs from the canonical sequence as follows:
     474-481: CEIIFCFF → FICSSYGD
     482-966: Missing.

Show »
Length:481
Mass (Da):53,299
Checksum:iFE3F3890EA24ED54
GO
Isoform 3 (identifier: O35245-3) [UniParc]FASTAAdd to basket
Also known as: delta7

The sequence of this isoform differs from the canonical sequence as follows:
     515-570: Missing.

Show »
Length:910
Mass (Da):102,420
Checksum:i0440C0F721450995
GO
Isoform 4 (identifier: O35245-4) [UniParc]FASTAAdd to basket
Also known as: delta9

The sequence of this isoform differs from the canonical sequence as follows:
     631-644: IFTQFRIILGDINF → IICSWRSSMIRTLK
     645-966: Missing.

Show »
Length:644
Mass (Da):72,702
Checksum:i10DCCE0B2DD5C4AD
GO
Isoform 5 (identifier: O35245-5) [UniParc]FASTAAdd to basket
Also known as: delta12/13

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

Note: Minor isoform.
Show »
Length:872
Mass (Da):98,082
Checksum:i855914112AD1FEB7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti365M → I in AAC53388 (PubMed:9339380).Curated1
Sequence conflicti370K → R in AAC53388 (PubMed:9339380).Curated1
Sequence conflicti560S → A in AAC53388 (PubMed:9339380).Curated1
Sequence conflicti688 – 689DL → SV in CAA74551 (PubMed:9716661).Curated2
Sequence conflicti746K → E in CAA73727 (PubMed:9716661).Curated1
Sequence conflicti746K → E in CAA74551 (PubMed:9716661).Curated1
Sequence conflicti746K → E in ACN11624 (PubMed:16192288).Curated1
Sequence conflicti800S → N in BAC35407 (PubMed:16141072).Curated1
Sequence conflicti942P → S in AAC53388 (PubMed:9339380).Curated1
Sequence conflicti957G → S in AAC53388 (PubMed:9339380).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_042485474 – 481CEIIFCFF → FICSSYGD in isoform 2. Curated8
Alternative sequenceiVSP_042486482 – 966Missing in isoform 2. CuratedAdd BLAST485
Alternative sequenceiVSP_042487515 – 570Missing in isoform 3. 1 PublicationAdd BLAST56
Alternative sequenceiVSP_042488631 – 644IFTQF…GDINF → IICSWRSSMIRTLK in isoform 4. CuratedAdd BLAST14
Alternative sequenceiVSP_042489645 – 966Missing in isoform 4. CuratedAdd BLAST322
Alternative sequenceiVSP_042490746 – 839Missing in isoform 5. CuratedAdd BLAST94

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19487.1. [O35245-1]
RefSeqiNP_032887.3. NM_008861.3. [O35245-1]
XP_006534878.1. XM_006534815.3. [O35245-3]
UniGeneiMm.483692.
Mm.6442.

Genome annotation databases

EnsembliENSMUST00000086831; ENSMUSP00000084041; ENSMUSG00000034462. [O35245-1]
GeneIDi18764.
KEGGimmu:18764.
UCSCiuc012eab.1. mouse. [O35245-1]
uc012eac.1. mouse. [O35245-3]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiPKD2_MOUSE
AccessioniPrimary (citable) accession number: O35245
Secondary accession number(s): C0KJK2
, E9Q4F6, E9QQA3, Q8BPR6, Q9ES37, Q9QWP0, Q9Z193, Q9Z194
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: July 5, 2017
This is version 161 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families