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O08852 (PKD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polycystin-1
Alternative name(s):
Autosomal dominant polycystic kidney disease 1 protein homolog
Gene names
Name:Pkd1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length4293 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in renal tubulogenesis. Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. Acts as a regulator of cilium length, together with PKD2. 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. May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate. Ref.3 Ref.6

Subunit structure

Interacts with PKD2. Interacts with PRKX; involved in differentiation and controlled morphogenesis of the kidney By similarity. Interacts with NPHP1 (via SH3 domain). Interacts with PKD2L1. Ref.4 Ref.7

Subcellular location

Membrane; Multi-pass membrane protein By similarity. Cell projectioncilium. Note: PKD1 localization to the plasma and ciliary membranes requires PKD2, is independent of PKD2 channel activity, and involves stimulation of PKD1 autocatalytic cleavage at the GPS domain By similarity. Ref.3

Domain

The LDL-receptor class A domain is atypical; the potential calcium-binding site is missing.

Post-translational modification

After synthesis, undergoes autoproteolytic cleavage between Leu-3040 and Thr-3041 in the GPS domain By similarity. Cleavage at the GPS domain occurs through a cis-autoproteolytic mechanism involving an ester-intermediate via N-O acyl rearrangement By similarity. This process takes place in the early secretory pathway, depends on initial N-glycosylation, and requires the REJ domain By similarity. PKD1 is ubiquitously and incompletely cleaved in wild-type mice, so that uncleaved and cleaved PKD1 molecules coexist. The differential patterns of cleavage during embryonic development, as well as in adult mice, suggest different functions of uncleaved and cleaved molecules. Ref.5

Disruption phenotype

Knockin mice expressing non-cleavable PKD1 show a hypomorphic phenotype. They are viable, show rapid cystic dilation in renal collecting duct and distal convoluted tubule, but not in the proximal portion of the nephron, during the postnatal period, and die with severe uremia, mostly at 3 weeks of age. Additionally, they show dilation of the common bile duct and intrahepatic biliary ducts, but develop a normal pancreas within their life span. Ref.5

Sequence similarities

Belongs to the polycystin family.

Contains 1 C-type lectin domain.

Contains 1 GPS domain.

Contains 1 LDL-receptor class A domain.

Contains 2 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Contains 16 PKD domains.

Contains 1 PLAT domain.

Contains 1 REJ domain.

Contains 1 WSC domain.

Ontologies

Keywords
   Cellular componentCell projection
Cilium
Membrane
   DomainCoiled coil
Leucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandLectin
   PTMAutocatalytic cleavage
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Inferred from direct assay PubMed 12007403. Source: MGI

blood vessel development

Inferred from mutant phenotype PubMed 10677526. Source: MGI

branching morphogenesis of an epithelial tube

Inferred from electronic annotation. Source: Ensembl

calcium ion transmembrane transport

Traceable author statement PubMed 12007403. Source: GOC

calcium ion transport

Inferred from mutant phenotype Ref.3. Source: MGI

cartilage condensation

Inferred from mutant phenotype PubMed 11593033. Source: MGI

cell cycle arrest

Inferred from direct assay PubMed 12007403. Source: MGI

cytoplasmic sequestering of transcription factor

Inferred from mutant phenotype PubMed 16311606. Source: BHF-UCL

detection of mechanical stimulus

Inferred from direct assay PubMed 15545994. Source: MGI

digestive tract development

Inferred from electronic annotation. Source: Ensembl

embryonic placenta development

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

genitalia development

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from mutant phenotype PubMed 11593033. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 16282979. Source: MGI

kidney development

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

liver development

Inferred from genetic interaction PubMed 21685914. Source: MGI

lung epithelium development

Inferred from electronic annotation. Source: Ensembl

mesonephric duct development

Inferred from electronic annotation. Source: Ensembl

metanephric ascending thin limb development

Inferred from electronic annotation. Source: Ensembl

metanephric collecting duct development

Inferred from electronic annotation. Source: Ensembl

metanephric distal tubule morphogenesis

Inferred from electronic annotation. Source: Ensembl

metanephric proximal tubule development

Inferred from electronic annotation. Source: Ensembl

neural tube development

Inferred from electronic annotation. Source: Ensembl

neuropeptide signaling pathway

Inferred from electronic annotation. Source: InterPro

nitrogen compound metabolic process

Inferred from genetic interaction PubMed 21685914. Source: MGI

peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB

placenta blood vessel development

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

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 cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein binding

Inferred from mutant phenotype PubMed 16311606. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

protein export from nucleus

Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB

regulation of mitotic spindle organization

Inferred from mutant phenotype PubMed 21685914. Source: MGI

regulation of proteasomal protein catabolic process

Inferred from mutant phenotype PubMed 23001567. Source: MGI

renal system development

Inferred from genetic interaction PubMed 21685914. Source: MGI

response to fluid shear stress

Inferred from mutant phenotype PubMed 18285569. Source: MGI

single organismal cell-cell adhesion

Inferred from mutant phenotype PubMed 10677526. Source: MGI

skin development

Inferred from electronic annotation. Source: Ensembl

spinal cord development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cilium

Inferred from direct assay Ref.3PubMed 18285569. Source: MGI

cytoplasm

Inferred from mutant phenotype PubMed 16311606. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

motile primary cilium

Inferred from direct assay PubMed 15858826. Source: MGI

nucleus

Inferred from direct assay PubMed 15545994. Source: MGI

polycystin complex

Inferred from direct assay PubMed 11901144. Source: MGI

   Molecular_functioncalcium channel activity

Traceable author statement PubMed 12007403. Source: MGI

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 22795130. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 42934270Polycystin-1
PRO_0000354054

Regions

Transmembrane3067 – 308721Helical; Potential
Transmembrane3273 – 329321Helical; Potential
Transmembrane3316 – 333621Helical; Potential
Transmembrane3550 – 357021Helical; Potential
Transmembrane3573 – 359321Helical; Potential
Transmembrane3664 – 368421Helical; Potential
Transmembrane3887 – 390721Helical; Potential
Transmembrane3929 – 394921Helical; Potential
Transmembrane3970 – 399021Helical; Potential
Transmembrane4018 – 403821Helical; Potential
Transmembrane4075 – 409521Helical; Potential
Domain24 – 6744LRRNT
Repeat68 – 9124LRR 1
Repeat92 – 11322LRR 2
Domain125 – 17854LRRCT
Domain177 – 27195WSC
Domain272 – 35988PKD 1
Domain415 – 530116C-type lectin
Domain633 – 66634LDL-receptor class A; atypical
Domain849 – 92274PKD 2
Domain929 – 101486PKD 3
Domain1017 – 1123107PKD 4
Domain1121 – 120989PKD 5
Domain1207 – 129286PKD 6
Domain1288 – 137790PKD 7
Domain1376 – 146388PKD 8
Domain1462 – 154584PKD 9
Domain1544 – 162986PKD 10
Domain1630 – 171889PKD 11
Domain1716 – 180287PKD 12
Domain1804 – 188683PKD 13
Domain1885 – 197086PKD 14
Domain1972 – 205382PKD 15
Domain2056 – 214489PKD 16
Domain2142 – 2828687REJ
Domain3004 – 305350GPS
Domain3110 – 3225116PLAT
Coiled coil4210 – 424132 Potential
Motif3734 – 374613Polycystin motif
Compositional bias3581 – 35855Poly-Ser
Compositional bias4153 – 419442Ser-rich

Sites

Site3040 – 30412Cleavage; by autolysis By similarity

Amino acid modifications

Modified residue41561Phosphoserine; by PRKX; in vitro By similarity
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation6271N-linked (GlcNAc...) Potential
Glycosylation6621N-linked (GlcNAc...) Potential
Glycosylation7401N-linked (GlcNAc...) Potential
Glycosylation8041N-linked (GlcNAc...) Potential
Glycosylation8351N-linked (GlcNAc...) Potential
Glycosylation8481N-linked (GlcNAc...) Potential
Glycosylation8591N-linked (GlcNAc...) Potential
Glycosylation8841N-linked (GlcNAc...) Potential
Glycosylation9151N-linked (GlcNAc...) Potential
Glycosylation9981N-linked (GlcNAc...) Potential
Glycosylation10041N-linked (GlcNAc...) Potential
Glycosylation10281N-linked (GlcNAc...) Potential
Glycosylation10841N-linked (GlcNAc...) Potential
Glycosylation10961N-linked (GlcNAc...) Potential
Glycosylation11071N-linked (GlcNAc...) Potential
Glycosylation11721N-linked (GlcNAc...) Potential
Glycosylation11881N-linked (GlcNAc...) Potential
Glycosylation12341N-linked (GlcNAc...) Potential
Glycosylation12631N-linked (GlcNAc...) Potential
Glycosylation13301N-linked (GlcNAc...) Potential
Glycosylation13421N-linked (GlcNAc...) Potential
Glycosylation13761N-linked (GlcNAc...) Potential
Glycosylation14441N-linked (GlcNAc...) Potential
Glycosylation14491N-linked (GlcNAc...) Potential
Glycosylation14681N-linked (GlcNAc...) Potential
Glycosylation15351N-linked (GlcNAc...) Potential
Glycosylation15481N-linked (GlcNAc...) Potential
Glycosylation15571N-linked (GlcNAc...) Potential
Glycosylation16431N-linked (GlcNAc...) Potential
Glycosylation16571N-linked (GlcNAc...) Potential
Glycosylation17061N-linked (GlcNAc...) Potential
Glycosylation17301N-linked (GlcNAc...) Potential
Glycosylation17881N-linked (GlcNAc...) Potential
Glycosylation18311N-linked (GlcNAc...) Potential
Glycosylation18631N-linked (GlcNAc...) Potential
Glycosylation18761N-linked (GlcNAc...) Potential
Glycosylation19871N-linked (GlcNAc...) Potential
Glycosylation20461N-linked (GlcNAc...) Potential
Glycosylation20701N-linked (GlcNAc...) Potential
Glycosylation21211N-linked (GlcNAc...) Potential
Glycosylation22441N-linked (GlcNAc...) Potential
Glycosylation23491N-linked (GlcNAc...) Potential
Glycosylation23911N-linked (GlcNAc...) Potential
Glycosylation24081N-linked (GlcNAc...) Potential
Glycosylation24141N-linked (GlcNAc...) Potential
Glycosylation25631N-linked (GlcNAc...) Potential
Glycosylation26401N-linked (GlcNAc...) Potential
Glycosylation27131N-linked (GlcNAc...) Potential
Glycosylation27491N-linked (GlcNAc...) Potential
Glycosylation28131N-linked (GlcNAc...) Potential
Glycosylation28361N-linked (GlcNAc...) Potential
Glycosylation28731N-linked (GlcNAc...) Potential
Glycosylation29481N-linked (GlcNAc...) Potential
Glycosylation29861N-linked (GlcNAc...) Potential
Glycosylation31391N-linked (GlcNAc...) Potential
Glycosylation37281N-linked (GlcNAc...) Potential
Glycosylation37801N-linked (GlcNAc...) Potential
Disulfide bond436 ↔ 529 By similarity
Disulfide bond507 ↔ 521 By similarity
Disulfide bond635 ↔ 648 By similarity
Disulfide bond642 ↔ 660 By similarity

Experimental info

Sequence conflict31L → P in AAC53207. Ref.1
Sequence conflict7711R → Q in AAC53207. Ref.1
Sequence conflict8711E → D in AAC53207. Ref.1
Sequence conflict11801A → T in AAC53207. Ref.1
Sequence conflict12921H → R in AAC53207. Ref.1
Sequence conflict16321A → V in AAC53207. Ref.1
Sequence conflict16841S → A in AAC53207. Ref.1
Sequence conflict17701A → T in AAC53207. Ref.1
Sequence conflict20851R → C in AAC53207. Ref.1
Sequence conflict25071A → V in AAC53207. Ref.1
Sequence conflict39561F → C in AAC53207. Ref.1
Sequence conflict39621R → H in AAC53207. Ref.1
Sequence conflict42371Q → R in AAC53207. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08852 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: FA12403171DBBCE0

FASTA4,293466,577
        10         20         30         40         50         60 
MPLGAPALLA LALGLGLWLG ALAGDPGRGC GPCPLPCFCG PAPDAACRVN CSGRWLQTLG 

        70         80         90        100        110        120 
PSLRIPADAT ALDLSHNLLQ TLDIGLLVNL SALVELDLSN NRISTLEEGV FANLFNLSEI 

       130        140        150        160        170        180 
NLSGNPFECN CGLAWLPRWA KEHQVHVVQS EATTCRGPIP LAGQPLLSIP LLDNACGEEY 

       190        200        210        220        230        240 
VACLPDNSSG AVAAVPFYFA HEGPLETEAC SAFCFSAGEG LAALSEQNQC LCGAGQASNS 

       250        260        270        280        290        300 
SAACSSWCSS ISLSLNSACG GPTLLQHTFP ASPGATLVGP HGPLASGQPA DFHITSSLPI 

       310        320        330        340        350        360 
SSTRWNFGDG SPEVDMASPA ATHFYVLPGS YHMTVVLALG AGSALLETEV QVEATPTVLE 

       370        380        390        400        410        420 
LVCPSFVHSN ESLELGIRHR GGSALEVTYS ILALDKEPAQ VVHPLCPLDT EIFPGNGHCY 

       430        440        450        460        470        480 
RLVAEKAPWL QAQEQCRTWA GAALAMVDSP AIQHFLVSKV TRSLDVWIGF SSVEGTEGLD 

       490        500        510        520        530        540 
PRGEAFSLES CQNWLPGEPH PATAEHCVRL GPAGQCNTDL CSAPHSYVCE LRPGGPVWDT 

       550        560        570        580        590        600 
ENFVMGMSGG GLSGPLHPLA QQETVQGPLR PVEVMVFPGL SPSREAFLTA AEFSTQKLEE 

       610        620        630        640        650        660 
PAQMRLQVYR PSGGAAAVPE GSSEPDNRTE PAPKCVPEEL WCPGANVCIP FDASCNSHVC 

       670        680        690        700        710        720 
INGSVSRLGL SRASYTLWKE FFFSVPAGPP TQYLVTLHSQ DVPMLPGDLI GLQHDAGPGT 

       730        740        750        760        770        780 
LLQCPLASSC PGQALYLSTN ASDWMTNLPV HLEEAWAGPV CSLQLLLVTE RLTPLLGLGP 

       790        800        810        820        830        840 
NPGLQHPGHY EVRATVGNSV SRQNLSCSFS VVSPIAGLRV IHPIPLDGHI YVPTNGSVLV 

       850        860        870        880        890        900 
LQVDSGANAT ATAQWFGGNI SAPFEDACPP EVDFLKQDCT EEANGTLFSV LMLPRLKEGD 

       910        920        930        940        950        960 
HTVEIVAQNG ASQANLSLRV TAEEPICGLR AVPSPEARVL QGILVRYSPM VEAGSDVAFR 

       970        980        990       1000       1010       1020 
WTIDDKQSLT FHNTVFNVIY QSAAIFKLSL TASNHVSNIT VNYNVTVERM NKMHGLWVSA 

      1030       1040       1050       1060       1070       1080 
VPTVLPPNAT LALTGGVLVD SAVEVAFLWN FGDGEQVLRQ FKPPYDESFQ VPDPTVAQVL 

      1090       1100       1110       1120       1130       1140 
VEHNTTHIYT TPGEYNLTVL VSNTYENLTQ QVTVSVRTVL PNVAIGMSSN VLVAGQPITF 

      1150       1160       1170       1180       1190       1200 
SPYPLPSTDG VLYTWDFGDG SPVLIQSQPV LNHTYSMTGA YRITLEVNNT VSSVTAHADI 

      1210       1220       1230       1240       1250       1260 
RVFQELHGLT VYLSPSVEQG APMVVSASVE SGDNITWTFD MGDGTVFTGP EATVQHVYLR 

      1270       1280       1290       1300       1310       1320 
AQNFTVTVEA ANPAGHLSQS LHVQVFVLEV LHIEPSTCIP TQPSAQLMAH VTGDPVHYLF 

      1330       1340       1350       1360       1370       1380 
DWTFGDGSSN VTVHGHPSVT HNFTRSGIFP LALVLSSHVN KAHYFTSICV EPEIRNITLQ 

      1390       1400       1410       1420       1430       1440 
PERQFVKLGD EARLVAYSWP PFPYRYTWDF GTEDTTHTQT GGSEVKFIYR EPGSYLVIVT 

      1450       1460       1470       1480       1490       1500 
VSNNISSTND SAFVEVQEPV LVTGIRINGS HVLELQQPYL LSAMGSGSPA TYLWELGDGS 

      1510       1520       1530       1540       1550       1560 
QSEGPEVTHI YSSTGDFTVR VSGWNEVSRS EAQLNITVKQ RVRGLTINAS RTVVPLNGSV 

      1570       1580       1590       1600       1610       1620 
SFSTLLEVGS DVHYSWVLCD RCTPIPGGPT ISYTFRSVGT FNIIVTAENE VGSAQDSIFI 

      1630       1640       1650       1660       1670       1680 
YVLQFIEGLQ VAGGDNGCCF PTNYTLQLQA AVRDGTNISY SWTAQQEGSL ITLFGSGKCF 

      1690       1700       1710       1720       1730       1740 
SLTSLKASTY YVHLRATNML GSAAANRTID FVEPVESLIL SASPNPAAVN MSLTLCAELA 

      1750       1760       1770       1780       1790       1800 
GGSGVVYTWY LEEGLSWKTS MPSTTHTFAA PGLHLVRVTA ENQLGSVNAT VEVAIQVPVG 

      1810       1820       1830       1840       1850       1860 
GLSIRTSEPD SIFVAAGSTL PFWGQLAEGT NVTWCWTLPG GSKDSQYIAV RFSTAGSFSL 

      1870       1880       1890       1900       1910       1920 
QLNASNAVSW VSAMYNLTVE EPIVNLMLWA SSKVVAPGQP VHFEILLAAG SALTFRLQVG 

      1930       1940       1950       1960       1970       1980 
GSVPEVLPSP HFSHSFFRVG DHLVNVQAEN HVSHAQAQVR ILVLEAVVGL QVPNCCEPGM 

      1990       2000       2010       2020       2030       2040 
ATGTEKNFTA RVQRGSRVAY AWYFSLQKVQ GDSLVILSGR DVTYTPVAAG LLEIHVRAFN 

      2050       2060       2070       2080       2090       2100 
ELGGVNLTLM VEVQDIIQYV TLQSGRCFTN RSARFEAATS PSPRRVTYHW DFGDGTPVQK 

      2110       2120       2130       2140       2150       2160 
TEEFWADHYY LRPGDYHVEV NATNLVSFFV AQATVTVQVL ACREPEVEVA LPLQVLMRRS 

      2170       2180       2190       2200       2210       2220 
QRNYLEAHVD LRNCVSYQTE YRWEIYRTAS CQRPGRMAQM VLPGVDVSRP QLVVPRLALP 

      2230       2240       2250       2260       2270       2280 
VGHYCFVFVV SFGDTPLARS IQANVTVAAE RLVPIIEGGS YRVWSDTQDL VLDGSKSYDP 

      2290       2300       2310       2320       2330       2340 
NLEDGDQTPL NFHWACVAST QSETGGCVLN FGPRGSSVVT IPLERLEAGV EYTFNLIVWK 

      2350       2360       2370       2380       2390       2400 
AGRKEEATNQ TVLIRSGRVP IVSLECVSCK AQAVYEVSRS SYVYLEGHCH NCSRGYKQGC 

      2410       2420       2430       2440       2450       2460 
WAARTFSNKT LVLNETTTST GSTGMNLVVR PGALRDGEGY IFTLTVLGHS GEEEGCASIR 

      2470       2480       2490       2500       2510       2520 
LSPNRPPLGG SCRLFPLDSV RGLTTKVHFE CTGWRDAEDG GAPLVYALLL KRCRQSYCEN 

      2530       2540       2550       2560       2570       2580 
FCIYKGSLST YGAVLPPGFQ PLFVVSLAVV VQDQLGAAVV ALNRSLTIVL PEPSGNPADL 

      2590       2600       2610       2620       2630       2640 
VPWLHSLTAS VLPGLLKQAD PQHVIEYSLA LITVLNEYEQ APDVSEPNVE QQLRAQMRKN 

      2650       2660       2670       2680       2690       2700 
ITETLISLRV NTVDDIQQIT AALAQCMVSS RELMCRSCLK KMLQKLEGMM RILQAETTEG 

      2710       2720       2730       2740       2750       2760 
TLTPTTIADS ILNITGDLIH LASLDMQGPQ PLELGVEPPS LMVASKAYNL SSALMRILMR 

      2770       2780       2790       2800       2810       2820 
SRVLNEEPLT LAGEEIVALG KRSDPLSLLC YGKALGPSCH FSIPEAFSGA LSNLSDVVQL 

      2830       2840       2850       2860       2870       2880 
IFLVDSNPFP FGYISNYTVS TKVASMAFQT QTGTQIPIEQ LAAERAITVK VPNNSDQAAQ 

      2890       2900       2910       2920       2930       2940 
SSHNPVGSTI VQPQTSVSAV VTADNSNPQA GLHLRITYTV LNERYLSAEP EPYLAVYLHS 

      2950       2960       2970       2980       2990       3000 
VSQPNEYNCS ASRRISLEVL EGADHRLYTF FIAPGTGTLD RSYYLNLTSH FHWSALEVSV 

      3010       3020       3030       3040       3050       3060 
GLYTSLCQYF SEEMMMWRTE GIVPLEETSP SQAVCLTRHL TAFGASLFVP PSHVQFIFPE 

      3070       3080       3090       3100       3110       3120 
PSASINYIVL LTCVICLVTY VVMAMILRKL DQLDVSRVRV IPFCGKGGRF KYEILVKTGW 

      3130       3140       3150       3160       3170       3180 
SRGSGTTAHV GIMLYGEDNR SGHRHLDGDR AFHRNSLDIF QIATPHSLGS VWKIRVWHDN 

      3190       3200       3210       3220       3230       3240 
KGLSPAWFLQ HIIVRDLQSA RSTFFLVNDW LSVETEANGG LVEKEVLAAN EAALWQFQRL 

      3250       3260       3270       3280       3290       3300 
LVAELQRGFF DKHIWLSIWD RPPRSRFTRV QRVTCCVLLL CLFLAANAVW YGVVRDTTYS 

      3310       3320       3330       3340       3350       3360 
MGPVSSLISP GVDTVAIGLV SSVVVYPVYL AVLFLFRMSR SKVSGDQNPT PTGQQALDVD 

      3370       3380       3390       3400       3410       3420 
SYLDPSVLDS SLLTLSGLTE AFAGQVKNDL FLEDAKSLVC WPSSEGTLSW PDLLSDPSVV 

      3430       3440       3450       3460       3470       3480 
SSTLQRLTQG RPGCMLGSEE DGASLVSPSL PAKYLSASDE DLIHQVLADG ANNLVPTQDT 

      3490       3500       3510       3520       3530       3540 
LLETDLLTSL SSVPGEKTET LILQTVGEER PASMGLSWEQ SPVTRLSRTG LVEGFQKRLL 

      3550       3560       3570       3580       3590       3600 
PAWCAPLAHG LSLLLVAVAV AVSGWIGASF PPSVSVMWLL SSSSSFLASF LGWEPLKVLL 

      3610       3620       3630       3640       3650       3660 
EALYFSLVAK RLHPDEDDTL VESPAVTPVS ERVPRVRPPH GFALFLAKEE ARKVKRLHDM 

      3670       3680       3690       3700       3710       3720 
LKRLLVYMLF LLVTLLANYG DASCHGHAYR LQSAIKQELD SQAFLAITRS DEFWPWMSHV 

      3730       3740       3750       3760       3770       3780 
FLPYVHGNQS SPELGPPRLR QVRLQEAFCP DPSSSEHMCS AAGSLSTSDY GIGWQSVVQN 

      3790       3800       3810       3820       3830       3840 
GSETWAYSAP DLLGAWYWGY CAVYDSGGYI QELGLSLEES RARLGFLQLH NWLDSRSRAV 

      3850       3860       3870       3880       3890       3900 
FVELTRYSPA VGLHAAVTLR LEFPVAGHAL AAFSVRPFAL RRLSTGLSLP LLTSVCLLLF 

      3910       3920       3930       3940       3950       3960 
ALYFSMAEVQ TWRKDGCACT ARPDTWARCL LVILTAATGL VRLAQLGIAD RQWTHFVQDH 

      3970       3980       3990       4000       4010       4020 
PRHFTSFDQV AQLGSVARGL AASLLFLLLV KAAQQLRFVR QWSVFGKTLC RALPELMGAT 

      4030       4040       4050       4060       4070       4080 
LGLVLLGVAY AQMAILLISS GADTLYNMAR AFLVLCPGAR VPTLCPSESW YLSPLLCVGL 

      4090       4100       4110       4120       4130       4140 
WALRVWGALR LGAILLRWRY HALRGELYRP AWEPQDYEMV ELFLRRLRLW MGFSKVKEFR 

      4150       4160       4170       4180       4190       4200 
HKVRFEGMDP LPSRSSRGSK SSPVVLPPSS GSEASHPSTS SSQPDGPSAS LSRSTLKLEP 

      4210       4220       4230       4240       4250       4260 
EPSRLHAVFE SLLVQFDRLN QATEDVYQLE QQLQSLQGHG HNGPPSSPSP GCFPGSQPAL 

      4270       4280       4290 
PSRLSRASQG LDQTVGPNRV SLWPNNKVHP SST 

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References

« Hide 'large scale' references
[1]"The mouse homolog of PKD1: sequence analysis and alternative splicing."
Lohning C., Nowicka U., Frischauf A.M.
Mamm. Genome 8:307-311(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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.
[3]"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.
[4]"Genomic organization and functional analysis of murine PKD2L1."
Murakami M., Ohba T., Xu F., Shida S., Satoh E., Ono K., Miyoshi I., Watanabe H., Ito H., Iijima T.
J. Biol. Chem. 280:5626-5635(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PKD2L1.
[5]"Essential role of cleavage of Polycystin-1 at G protein-coupled receptor proteolytic site for kidney tubular structure."
Yu S., Hackmann K., Gao J., He X., Piontek K., Garcia-Gonzalez M.A., Menezes L.F., Xu H., Germino G.G., Zuo J., Qian F.
Proc. Natl. Acad. Sci. U.S.A. 104:18688-18693(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, DIFFERENTIAL PATTERN OF AUTOCLEAVAGE.
[6]"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.
[7]"Nephrocystin-1 forms a complex with polycystin-1 via a polyproline motif/SH3 domain interaction and regulates the apoptotic response in mammals."
Wodarczyk C., Distefano G., Rowe I., Gaetani M., Bricoli B., Muorah M., Spitaleri A., Mannella V., Ricchiuto P., Pema M., Castelli M., Casanova A.E., Mollica L., Banzi M., Boca M., Antignac C., Saunier S., Musco G., Boletta A.
PLoS ONE 5:E12719-E12719(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NPHP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U70209 mRNA. Translation: AAC53207.1.
AC132367 Genomic DNA. No translation available.
CCDSCCDS28485.1.
RefSeqNP_038658.2. NM_013630.2.
UniGeneMm.290442.
Mm.30435.

3D structure databases

ProteinModelPortalO08852.
SMRO08852. Positions 275-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202204. 3 interactions.
DIPDIP-44233N.
IntActO08852. 4 interactions.
MINTMINT-5163387.

Protein family/group databases

MEROPST06.001.

PTM databases

PhosphoSiteO08852.

Proteomic databases

PRIDEO08852.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035565; ENSMUSP00000049296; ENSMUSG00000032855.
GeneID18763.
KEGGmmu:18763.
UCSCuc008awv.1. mouse.

Organism-specific databases

CTD5310.
MGIMGI:97603. Pkd1.

Phylogenomic databases

eggNOGCOG3291.
GeneTreeENSGT00730000110796.
HOGENOMHOG000168445.
HOVERGENHBG049412.
InParanoidO08852.
KOK04985.
OMAGQCNTDL.
OrthoDBEOG76X5Z6.
TreeFamTF316484.

Gene expression databases

ArrayExpressO08852.
BgeeO08852.
GenevestigatorO08852.

Family and domain databases

Gene3D2.60.40.670. 13 hits.
2.60.60.20. 1 hit.
3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR000483. Cys-rich_flank_reg_C.
IPR000203. GPS.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR008976. Lipase_LipOase.
IPR000372. LRR-contain_N.
IPR022409. PKD/Chitinase_dom.
IPR002859. PKD/REJ-like.
IPR013122. PKD1_2_channel.
IPR000434. PKD_1.
IPR000601. PKD_dom.
IPR001024. PLAT/LH2_dom.
IPR006228. Polycystin_cat.
IPR014010. REJ-like.
IPR002889. WSC_carb-bd.
IPR013994. WSC_carb-bd_subgr.
[Graphical view]
PfamPF01825. GPS. 1 hit.
PF00059. Lectin_C. 1 hit.
PF13855. LRR_8. 1 hit.
PF00801. PKD. 15 hits.
PF08016. PKD_channel. 1 hit.
PF01477. PLAT. 1 hit.
PF02010. REJ. 1 hit.
PF01822. WSC. 1 hit.
[Graphical view]
PRINTSPR00500. POLYCYSTIN1.
SMARTSM00034. CLECT. 1 hit.
SM00303. GPS. 1 hit.
SM00308. LH2. 1 hit.
SM00369. LRR_TYP. 1 hit.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00089. PKD. 15 hits.
SM00321. WSC. 1 hit.
[Graphical view]
SUPFAMSSF49299. SSF49299. 13 hits.
SSF49723. SSF49723. 1 hit.
SSF56436. SSF56436. 1 hit.
TIGRFAMsTIGR00864. PCC. 1 hit.
PROSITEPS50041. C_TYPE_LECTIN_2. 1 hit.
PS50221. GPS. 1 hit.
PS51450. LRR. 3 hits.
PS50093. PKD. 12 hits.
PS50095. PLAT. 1 hit.
PS51111. REJ. 1 hit.
PS51212. WSC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPkd1. mouse.
NextBio294959.
PROO08852.
SOURCESearch...

Entry information

Entry namePKD1_MOUSE
AccessionPrimary (citable) accession number: O08852
Secondary accession number(s): E9QJR6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 115 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