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O08852

- PKD1_MOUSE

UniProt

O08852 - PKD1_MOUSE

Protein

Polycystin-1

Gene

Pkd1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei3040 – 30412Cleavage; by autolysisBy similarity

    GO - Molecular functioni

    1. calcium channel activity Source: MGI
    2. carbohydrate binding Source: InterPro
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. blood vessel development Source: MGI
    2. branching morphogenesis of an epithelial tube Source: Ensembl
    3. calcium ion transmembrane transport Source: GOC
    4. calcium ion transport Source: MGI
    5. cartilage condensation Source: MGI
    6. cell cycle arrest Source: MGI
    7. cytoplasmic sequestering of transcription factor Source: BHF-UCL
    8. detection of mechanical stimulus Source: MGI
    9. digestive tract development Source: Ensembl
    10. embryonic placenta development Source: BHF-UCL
    11. genitalia development Source: Ensembl
    12. heart development Source: MGI
    13. in utero embryonic development Source: MGI
    14. JAK-STAT cascade Source: MGI
    15. kidney development Source: BHF-UCL
    16. liver development Source: MGI
    17. lung epithelium development Source: Ensembl
    18. mesonephric duct development Source: Ensembl
    19. metanephric ascending thin limb development Source: Ensembl
    20. metanephric collecting duct development Source: Ensembl
    21. metanephric distal tubule morphogenesis Source: Ensembl
    22. metanephric proximal tubule development Source: Ensembl
    23. neural tube development Source: Ensembl
    24. neuropeptide signaling pathway Source: InterPro
    25. nitrogen compound metabolic process Source: MGI
    26. peptidyl-serine phosphorylation Source: UniProtKB
    27. placenta blood vessel development Source: BHF-UCL
    28. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
    29. positive regulation of cytosolic calcium ion concentration Source: Ensembl
    30. positive regulation of protein binding Source: BHF-UCL
    31. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    32. protein export from nucleus Source: UniProtKB
    33. regulation of mitotic spindle organization Source: MGI
    34. regulation of proteasomal protein catabolic process Source: MGI
    35. renal system development Source: MGI
    36. response to fluid shear stress Source: MGI
    37. single organismal cell-cell adhesion Source: MGI
    38. skin development Source: Ensembl
    39. spinal cord development Source: Ensembl

    Keywords - Ligandi

    Lectin

    Protein family/group databases

    MEROPSiT06.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polycystin-1
    Alternative name(s):
    Autosomal dominant polycystic kidney disease 1 protein homolog
    Gene namesi
    Name:Pkd1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:97603. Pkd1.

    Subcellular locationi

    Membrane By similarity; Multi-pass membrane protein By similarity. Cell projectioncilium 1 Publication
    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

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. cilium Source: MGI
    3. cytoplasm Source: BHF-UCL
    4. Golgi apparatus Source: Ensembl
    5. integral component of membrane Source: UniProtKB-KW
    6. lateral plasma membrane Source: Ensembl
    7. motile primary cilium Source: MGI
    8. nucleus Source: MGI
    9. polycystin complex Source: MGI

    Keywords - Cellular componenti

    Cell projection, Cilium, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 42934270Polycystin-1PRO_0000354054Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi436 ↔ 529By similarity
    Disulfide bondi507 ↔ 521By similarity
    Glycosylationi627 – 6271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi635 ↔ 648By similarity
    Disulfide bondi642 ↔ 660By similarity
    Glycosylationi662 – 6621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi740 – 7401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi804 – 8041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi835 – 8351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi848 – 8481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi859 – 8591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi884 – 8841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi915 – 9151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi998 – 9981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1004 – 10041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1028 – 10281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1084 – 10841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1096 – 10961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1107 – 11071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1172 – 11721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1188 – 11881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1234 – 12341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1263 – 12631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1330 – 13301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1342 – 13421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1376 – 13761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1444 – 14441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1449 – 14491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1468 – 14681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1535 – 15351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1548 – 15481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1557 – 15571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1643 – 16431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1657 – 16571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1706 – 17061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1730 – 17301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1788 – 17881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1831 – 18311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1863 – 18631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1876 – 18761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1987 – 19871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2046 – 20461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2070 – 20701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2121 – 21211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2244 – 22441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2349 – 23491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2391 – 23911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2408 – 24081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2414 – 24141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2563 – 25631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2640 – 26401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2713 – 27131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2749 – 27491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2813 – 28131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2836 – 28361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2873 – 28731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2948 – 29481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2986 – 29861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3139 – 31391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3728 – 37281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3780 – 37801N-linked (GlcNAc...)Sequence Analysis
    Modified residuei4156 – 41561Phosphoserine; by PRKX; in vitroBy similarity

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiO08852.

    PTM databases

    PhosphoSiteiO08852.

    Expressioni

    Gene expression databases

    ArrayExpressiO08852.
    BgeeiO08852.
    GenevestigatoriO08852.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi202204. 3 interactions.
    DIPiDIP-44233N.
    IntActiO08852. 4 interactions.
    MINTiMINT-5163387.

    Structurei

    3D structure databases

    ProteinModelPortaliO08852.
    SMRiO08852. Positions 275-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei3067 – 308721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3273 – 329321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3316 – 333621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3550 – 357021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3573 – 359321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3664 – 368421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3887 – 390721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3929 – 394921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3970 – 399021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4018 – 403821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4075 – 409521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 6744LRRNTAdd
    BLAST
    Repeati68 – 9124LRR 1Add
    BLAST
    Repeati92 – 11322LRR 2Add
    BLAST
    Domaini125 – 17854LRRCTAdd
    BLAST
    Domaini177 – 27195WSCPROSITE-ProRule annotationAdd
    BLAST
    Domaini272 – 35988PKD 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini415 – 530116C-type lectinPROSITE-ProRule annotationAdd
    BLAST
    Domaini633 – 66634LDL-receptor class A; atypicalAdd
    BLAST
    Domaini849 – 92274PKD 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini929 – 101486PKD 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1017 – 1123107PKD 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1121 – 120989PKD 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1207 – 129286PKD 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1288 – 137790PKD 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1376 – 146388PKD 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1462 – 154584PKD 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1544 – 162986PKD 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1630 – 171889PKD 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1716 – 180287PKD 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1804 – 188683PKD 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1885 – 197086PKD 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1972 – 205382PKD 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini2056 – 214489PKD 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini2142 – 2828687REJPROSITE-ProRule annotationAdd
    BLAST
    Domaini3004 – 305350GPSPROSITE-ProRule annotationAdd
    BLAST
    Domaini3110 – 3225116PLATPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili4210 – 424132Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi3734 – 374613Polycystin motifAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi3581 – 35855Poly-Ser
    Compositional biasi4153 – 419442Ser-richAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the polycystin family.Curated
    Contains 1 C-type lectin domain.PROSITE-ProRule annotation
    Contains 1 GPS domain.PROSITE-ProRule annotation
    Contains 1 LDL-receptor class A domain.Curated
    Contains 2 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated
    Contains 1 LRRNT domain.Curated
    Contains 16 PKD domains.PROSITE-ProRule annotation
    Contains 1 PLAT domain.PROSITE-ProRule annotation
    Contains 1 REJ domain.PROSITE-ProRule annotation
    Contains 1 WSC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3291.
    GeneTreeiENSGT00730000110796.
    HOGENOMiHOG000168445.
    HOVERGENiHBG049412.
    InParanoidiO08852.
    KOiK04985.
    OMAiGQCNTDL.
    OrthoDBiEOG76X5Z6.
    TreeFamiTF316484.

    Family and domain databases

    Gene3Di2.60.40.670. 13 hits.
    2.60.60.20. 1 hit.
    3.10.100.10. 1 hit.
    InterProiIPR001304. 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]
    PfamiPF01825. 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]
    PRINTSiPR00500. POLYCYSTIN1.
    SMARTiSM00034. 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]
    SUPFAMiSSF49299. SSF49299. 13 hits.
    SSF49723. SSF49723. 1 hit.
    SSF56436. SSF56436. 1 hit.
    TIGRFAMsiTIGR00864. PCC. 1 hit.
    PROSITEiPS50041. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O08852-1 [UniParc]FASTAAdd to Basket

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    MPLGAPALLA LALGLGLWLG ALAGDPGRGC GPCPLPCFCG PAPDAACRVN     50
    CSGRWLQTLG PSLRIPADAT ALDLSHNLLQ TLDIGLLVNL SALVELDLSN 100
    NRISTLEEGV FANLFNLSEI NLSGNPFECN CGLAWLPRWA KEHQVHVVQS 150
    EATTCRGPIP LAGQPLLSIP LLDNACGEEY VACLPDNSSG AVAAVPFYFA 200
    HEGPLETEAC SAFCFSAGEG LAALSEQNQC LCGAGQASNS SAACSSWCSS 250
    ISLSLNSACG GPTLLQHTFP ASPGATLVGP HGPLASGQPA DFHITSSLPI 300
    SSTRWNFGDG SPEVDMASPA ATHFYVLPGS YHMTVVLALG AGSALLETEV 350
    QVEATPTVLE LVCPSFVHSN ESLELGIRHR GGSALEVTYS ILALDKEPAQ 400
    VVHPLCPLDT EIFPGNGHCY RLVAEKAPWL QAQEQCRTWA GAALAMVDSP 450
    AIQHFLVSKV TRSLDVWIGF SSVEGTEGLD PRGEAFSLES CQNWLPGEPH 500
    PATAEHCVRL GPAGQCNTDL CSAPHSYVCE LRPGGPVWDT ENFVMGMSGG 550
    GLSGPLHPLA QQETVQGPLR PVEVMVFPGL SPSREAFLTA AEFSTQKLEE 600
    PAQMRLQVYR PSGGAAAVPE GSSEPDNRTE PAPKCVPEEL WCPGANVCIP 650
    FDASCNSHVC INGSVSRLGL SRASYTLWKE FFFSVPAGPP TQYLVTLHSQ 700
    DVPMLPGDLI GLQHDAGPGT LLQCPLASSC PGQALYLSTN ASDWMTNLPV 750
    HLEEAWAGPV CSLQLLLVTE RLTPLLGLGP NPGLQHPGHY EVRATVGNSV 800
    SRQNLSCSFS VVSPIAGLRV IHPIPLDGHI YVPTNGSVLV LQVDSGANAT 850
    ATAQWFGGNI SAPFEDACPP EVDFLKQDCT EEANGTLFSV LMLPRLKEGD 900
    HTVEIVAQNG ASQANLSLRV TAEEPICGLR AVPSPEARVL QGILVRYSPM 950
    VEAGSDVAFR WTIDDKQSLT FHNTVFNVIY QSAAIFKLSL TASNHVSNIT 1000
    VNYNVTVERM NKMHGLWVSA VPTVLPPNAT LALTGGVLVD SAVEVAFLWN 1050
    FGDGEQVLRQ FKPPYDESFQ VPDPTVAQVL VEHNTTHIYT TPGEYNLTVL 1100
    VSNTYENLTQ QVTVSVRTVL PNVAIGMSSN VLVAGQPITF SPYPLPSTDG 1150
    VLYTWDFGDG SPVLIQSQPV LNHTYSMTGA YRITLEVNNT VSSVTAHADI 1200
    RVFQELHGLT VYLSPSVEQG APMVVSASVE SGDNITWTFD MGDGTVFTGP 1250
    EATVQHVYLR AQNFTVTVEA ANPAGHLSQS LHVQVFVLEV LHIEPSTCIP 1300
    TQPSAQLMAH VTGDPVHYLF DWTFGDGSSN VTVHGHPSVT HNFTRSGIFP 1350
    LALVLSSHVN KAHYFTSICV EPEIRNITLQ PERQFVKLGD EARLVAYSWP 1400
    PFPYRYTWDF GTEDTTHTQT GGSEVKFIYR EPGSYLVIVT VSNNISSTND 1450
    SAFVEVQEPV LVTGIRINGS HVLELQQPYL LSAMGSGSPA TYLWELGDGS 1500
    QSEGPEVTHI YSSTGDFTVR VSGWNEVSRS EAQLNITVKQ RVRGLTINAS 1550
    RTVVPLNGSV SFSTLLEVGS DVHYSWVLCD RCTPIPGGPT ISYTFRSVGT 1600
    FNIIVTAENE VGSAQDSIFI YVLQFIEGLQ VAGGDNGCCF PTNYTLQLQA 1650
    AVRDGTNISY SWTAQQEGSL ITLFGSGKCF SLTSLKASTY YVHLRATNML 1700
    GSAAANRTID FVEPVESLIL SASPNPAAVN MSLTLCAELA GGSGVVYTWY 1750
    LEEGLSWKTS MPSTTHTFAA PGLHLVRVTA ENQLGSVNAT VEVAIQVPVG 1800
    GLSIRTSEPD SIFVAAGSTL PFWGQLAEGT NVTWCWTLPG GSKDSQYIAV 1850
    RFSTAGSFSL QLNASNAVSW VSAMYNLTVE EPIVNLMLWA SSKVVAPGQP 1900
    VHFEILLAAG SALTFRLQVG GSVPEVLPSP HFSHSFFRVG DHLVNVQAEN 1950
    HVSHAQAQVR ILVLEAVVGL QVPNCCEPGM ATGTEKNFTA RVQRGSRVAY 2000
    AWYFSLQKVQ GDSLVILSGR DVTYTPVAAG LLEIHVRAFN ELGGVNLTLM 2050
    VEVQDIIQYV TLQSGRCFTN RSARFEAATS PSPRRVTYHW DFGDGTPVQK 2100
    TEEFWADHYY LRPGDYHVEV NATNLVSFFV AQATVTVQVL ACREPEVEVA 2150
    LPLQVLMRRS QRNYLEAHVD LRNCVSYQTE YRWEIYRTAS CQRPGRMAQM 2200
    VLPGVDVSRP QLVVPRLALP VGHYCFVFVV SFGDTPLARS IQANVTVAAE 2250
    RLVPIIEGGS YRVWSDTQDL VLDGSKSYDP NLEDGDQTPL NFHWACVAST 2300
    QSETGGCVLN FGPRGSSVVT IPLERLEAGV EYTFNLIVWK AGRKEEATNQ 2350
    TVLIRSGRVP IVSLECVSCK AQAVYEVSRS SYVYLEGHCH NCSRGYKQGC 2400
    WAARTFSNKT LVLNETTTST GSTGMNLVVR PGALRDGEGY IFTLTVLGHS 2450
    GEEEGCASIR LSPNRPPLGG SCRLFPLDSV RGLTTKVHFE CTGWRDAEDG 2500
    GAPLVYALLL KRCRQSYCEN FCIYKGSLST YGAVLPPGFQ PLFVVSLAVV 2550
    VQDQLGAAVV ALNRSLTIVL PEPSGNPADL VPWLHSLTAS VLPGLLKQAD 2600
    PQHVIEYSLA LITVLNEYEQ APDVSEPNVE QQLRAQMRKN ITETLISLRV 2650
    NTVDDIQQIT AALAQCMVSS RELMCRSCLK KMLQKLEGMM RILQAETTEG 2700
    TLTPTTIADS ILNITGDLIH LASLDMQGPQ PLELGVEPPS LMVASKAYNL 2750
    SSALMRILMR SRVLNEEPLT LAGEEIVALG KRSDPLSLLC YGKALGPSCH 2800
    FSIPEAFSGA LSNLSDVVQL IFLVDSNPFP FGYISNYTVS TKVASMAFQT 2850
    QTGTQIPIEQ LAAERAITVK VPNNSDQAAQ SSHNPVGSTI VQPQTSVSAV 2900
    VTADNSNPQA GLHLRITYTV LNERYLSAEP EPYLAVYLHS VSQPNEYNCS 2950
    ASRRISLEVL EGADHRLYTF FIAPGTGTLD RSYYLNLTSH FHWSALEVSV 3000
    GLYTSLCQYF SEEMMMWRTE GIVPLEETSP SQAVCLTRHL TAFGASLFVP 3050
    PSHVQFIFPE PSASINYIVL LTCVICLVTY VVMAMILRKL DQLDVSRVRV 3100
    IPFCGKGGRF KYEILVKTGW SRGSGTTAHV GIMLYGEDNR SGHRHLDGDR 3150
    AFHRNSLDIF QIATPHSLGS VWKIRVWHDN KGLSPAWFLQ HIIVRDLQSA 3200
    RSTFFLVNDW LSVETEANGG LVEKEVLAAN EAALWQFQRL LVAELQRGFF 3250
    DKHIWLSIWD RPPRSRFTRV QRVTCCVLLL CLFLAANAVW YGVVRDTTYS 3300
    MGPVSSLISP GVDTVAIGLV SSVVVYPVYL AVLFLFRMSR SKVSGDQNPT 3350
    PTGQQALDVD SYLDPSVLDS SLLTLSGLTE AFAGQVKNDL FLEDAKSLVC 3400
    WPSSEGTLSW PDLLSDPSVV SSTLQRLTQG RPGCMLGSEE DGASLVSPSL 3450
    PAKYLSASDE DLIHQVLADG ANNLVPTQDT LLETDLLTSL SSVPGEKTET 3500
    LILQTVGEER PASMGLSWEQ SPVTRLSRTG LVEGFQKRLL PAWCAPLAHG 3550
    LSLLLVAVAV AVSGWIGASF PPSVSVMWLL SSSSSFLASF LGWEPLKVLL 3600
    EALYFSLVAK RLHPDEDDTL VESPAVTPVS ERVPRVRPPH GFALFLAKEE 3650
    ARKVKRLHDM LKRLLVYMLF LLVTLLANYG DASCHGHAYR LQSAIKQELD 3700
    SQAFLAITRS DEFWPWMSHV FLPYVHGNQS SPELGPPRLR QVRLQEAFCP 3750
    DPSSSEHMCS AAGSLSTSDY GIGWQSVVQN GSETWAYSAP DLLGAWYWGY 3800
    CAVYDSGGYI QELGLSLEES RARLGFLQLH NWLDSRSRAV FVELTRYSPA 3850
    VGLHAAVTLR LEFPVAGHAL AAFSVRPFAL RRLSTGLSLP LLTSVCLLLF 3900
    ALYFSMAEVQ TWRKDGCACT ARPDTWARCL LVILTAATGL VRLAQLGIAD 3950
    RQWTHFVQDH PRHFTSFDQV AQLGSVARGL AASLLFLLLV KAAQQLRFVR 4000
    QWSVFGKTLC RALPELMGAT LGLVLLGVAY AQMAILLISS GADTLYNMAR 4050
    AFLVLCPGAR VPTLCPSESW YLSPLLCVGL WALRVWGALR LGAILLRWRY 4100
    HALRGELYRP AWEPQDYEMV ELFLRRLRLW MGFSKVKEFR HKVRFEGMDP 4150
    LPSRSSRGSK SSPVVLPPSS GSEASHPSTS SSQPDGPSAS LSRSTLKLEP 4200
    EPSRLHAVFE SLLVQFDRLN QATEDVYQLE QQLQSLQGHG HNGPPSSPSP 4250
    GCFPGSQPAL PSRLSRASQG LDQTVGPNRV SLWPNNKVHP SST 4293
    Length:4,293
    Mass (Da):466,577
    Last modified:July 27, 2011 - v2
    Checksum:iFA12403171DBBCE0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31L → P in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti771 – 7711R → Q in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti871 – 8711E → D in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti1180 – 11801A → T in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti1292 – 12921H → R in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti1632 – 16321A → V in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti1684 – 16841S → A in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti1770 – 17701A → T in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti2085 – 20851R → C in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti2507 – 25071A → V in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti3956 – 39561F → C in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti3962 – 39621R → H in AAC53207. (PubMed:9107672)Curated
    Sequence conflicti4237 – 42371Q → R in AAC53207. (PubMed:9107672)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70209 mRNA. Translation: AAC53207.1.
    AC132367 Genomic DNA. No translation available.
    CCDSiCCDS28485.1.
    RefSeqiNP_038658.2. NM_013630.2.
    UniGeneiMm.290442.
    Mm.30435.

    Genome annotation databases

    EnsembliENSMUST00000035565; ENSMUSP00000049296; ENSMUSG00000032855.
    GeneIDi18763.
    KEGGimmu:18763.
    UCSCiuc008awv.1. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    Polycystin-1

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70209 mRNA. Translation: AAC53207.1 .
    AC132367 Genomic DNA. No translation available.
    CCDSi CCDS28485.1.
    RefSeqi NP_038658.2. NM_013630.2.
    UniGenei Mm.290442.
    Mm.30435.

    3D structure databases

    ProteinModelPortali O08852.
    SMRi O08852. Positions 275-354.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202204. 3 interactions.
    DIPi DIP-44233N.
    IntActi O08852. 4 interactions.
    MINTi MINT-5163387.

    Protein family/group databases

    MEROPSi T06.001.

    PTM databases

    PhosphoSitei O08852.

    Proteomic databases

    PRIDEi O08852.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000035565 ; ENSMUSP00000049296 ; ENSMUSG00000032855 .
    GeneIDi 18763.
    KEGGi mmu:18763.
    UCSCi uc008awv.1. mouse.

    Organism-specific databases

    CTDi 5310.
    MGIi MGI:97603. Pkd1.

    Phylogenomic databases

    eggNOGi COG3291.
    GeneTreei ENSGT00730000110796.
    HOGENOMi HOG000168445.
    HOVERGENi HBG049412.
    InParanoidi O08852.
    KOi K04985.
    OMAi GQCNTDL.
    OrthoDBi EOG76X5Z6.
    TreeFami TF316484.

    Miscellaneous databases

    ChiTaRSi Pkd1. mouse.
    NextBioi 294959.
    PROi O08852.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08852.
    Bgeei O08852.
    Genevestigatori O08852.

    Family and domain databases

    Gene3Di 2.60.40.670. 13 hits.
    2.60.60.20. 1 hit.
    3.10.100.10. 1 hit.
    InterProi IPR001304. 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 ]
    Pfami PF01825. 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 ]
    PRINTSi PR00500. POLYCYSTIN1.
    SMARTi SM00034. 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 ]
    SUPFAMi SSF49299. SSF49299. 13 hits.
    SSF49723. SSF49723. 1 hit.
    SSF56436. SSF56436. 1 hit.
    TIGRFAMsi TIGR00864. PCC. 1 hit.
    PROSITEi PS50041. 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 ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.

    Entry informationi

    Entry nameiPKD1_MOUSE
    AccessioniPrimary (citable) accession number: O08852
    Secondary accession number(s): E9QJR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 25, 2008
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 of the sequence. [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

    External Data

    Dasty 3