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O08852

- PKD1_MOUSE

UniProt

O08852 - PKD1_MOUSE

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Protein

Polycystin-1

Gene

Pkd1

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

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: UniProtKB-KW

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
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  5. Golgi apparatus Source: Ensembl
  6. integral component of membrane Source: UniProtKB-KW
  7. lateral plasma membrane Source: Ensembl
  8. motile primary cilium Source: MGI
  9. nucleus Source: MGI
  10. polycystin complex Source: MGI
Complete GO annotation...

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

BgeeiO08852.
ExpressionAtlasiO08852. baseline and differential.
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.
GeneTreeiENSGT00700000104221.
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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        10         20         30         40         50
MPLGAPALLA LALGLGLWLG ALAGDPGRGC GPCPLPCFCG PAPDAACRVN
60 70 80 90 100
CSGRWLQTLG PSLRIPADAT ALDLSHNLLQ TLDIGLLVNL SALVELDLSN
110 120 130 140 150
NRISTLEEGV FANLFNLSEI NLSGNPFECN CGLAWLPRWA KEHQVHVVQS
160 170 180 190 200
EATTCRGPIP LAGQPLLSIP LLDNACGEEY VACLPDNSSG AVAAVPFYFA
210 220 230 240 250
HEGPLETEAC SAFCFSAGEG LAALSEQNQC LCGAGQASNS SAACSSWCSS
260 270 280 290 300
ISLSLNSACG GPTLLQHTFP ASPGATLVGP HGPLASGQPA DFHITSSLPI
310 320 330 340 350
SSTRWNFGDG SPEVDMASPA ATHFYVLPGS YHMTVVLALG AGSALLETEV
360 370 380 390 400
QVEATPTVLE LVCPSFVHSN ESLELGIRHR GGSALEVTYS ILALDKEPAQ
410 420 430 440 450
VVHPLCPLDT EIFPGNGHCY RLVAEKAPWL QAQEQCRTWA GAALAMVDSP
460 470 480 490 500
AIQHFLVSKV TRSLDVWIGF SSVEGTEGLD PRGEAFSLES CQNWLPGEPH
510 520 530 540 550
PATAEHCVRL GPAGQCNTDL CSAPHSYVCE LRPGGPVWDT ENFVMGMSGG
560 570 580 590 600
GLSGPLHPLA QQETVQGPLR PVEVMVFPGL SPSREAFLTA AEFSTQKLEE
610 620 630 640 650
PAQMRLQVYR PSGGAAAVPE GSSEPDNRTE PAPKCVPEEL WCPGANVCIP
660 670 680 690 700
FDASCNSHVC INGSVSRLGL SRASYTLWKE FFFSVPAGPP TQYLVTLHSQ
710 720 730 740 750
DVPMLPGDLI GLQHDAGPGT LLQCPLASSC PGQALYLSTN ASDWMTNLPV
760 770 780 790 800
HLEEAWAGPV CSLQLLLVTE RLTPLLGLGP NPGLQHPGHY EVRATVGNSV
810 820 830 840 850
SRQNLSCSFS VVSPIAGLRV IHPIPLDGHI YVPTNGSVLV LQVDSGANAT
860 870 880 890 900
ATAQWFGGNI SAPFEDACPP EVDFLKQDCT EEANGTLFSV LMLPRLKEGD
910 920 930 940 950
HTVEIVAQNG ASQANLSLRV TAEEPICGLR AVPSPEARVL QGILVRYSPM
960 970 980 990 1000
VEAGSDVAFR WTIDDKQSLT FHNTVFNVIY QSAAIFKLSL TASNHVSNIT
1010 1020 1030 1040 1050
VNYNVTVERM NKMHGLWVSA VPTVLPPNAT LALTGGVLVD SAVEVAFLWN
1060 1070 1080 1090 1100
FGDGEQVLRQ FKPPYDESFQ VPDPTVAQVL VEHNTTHIYT TPGEYNLTVL
1110 1120 1130 1140 1150
VSNTYENLTQ QVTVSVRTVL PNVAIGMSSN VLVAGQPITF SPYPLPSTDG
1160 1170 1180 1190 1200
VLYTWDFGDG SPVLIQSQPV LNHTYSMTGA YRITLEVNNT VSSVTAHADI
1210 1220 1230 1240 1250
RVFQELHGLT VYLSPSVEQG APMVVSASVE SGDNITWTFD MGDGTVFTGP
1260 1270 1280 1290 1300
EATVQHVYLR AQNFTVTVEA ANPAGHLSQS LHVQVFVLEV LHIEPSTCIP
1310 1320 1330 1340 1350
TQPSAQLMAH VTGDPVHYLF DWTFGDGSSN VTVHGHPSVT HNFTRSGIFP
1360 1370 1380 1390 1400
LALVLSSHVN KAHYFTSICV EPEIRNITLQ PERQFVKLGD EARLVAYSWP
1410 1420 1430 1440 1450
PFPYRYTWDF GTEDTTHTQT GGSEVKFIYR EPGSYLVIVT VSNNISSTND
1460 1470 1480 1490 1500
SAFVEVQEPV LVTGIRINGS HVLELQQPYL LSAMGSGSPA TYLWELGDGS
1510 1520 1530 1540 1550
QSEGPEVTHI YSSTGDFTVR VSGWNEVSRS EAQLNITVKQ RVRGLTINAS
1560 1570 1580 1590 1600
RTVVPLNGSV SFSTLLEVGS DVHYSWVLCD RCTPIPGGPT ISYTFRSVGT
1610 1620 1630 1640 1650
FNIIVTAENE VGSAQDSIFI YVLQFIEGLQ VAGGDNGCCF PTNYTLQLQA
1660 1670 1680 1690 1700
AVRDGTNISY SWTAQQEGSL ITLFGSGKCF SLTSLKASTY YVHLRATNML
1710 1720 1730 1740 1750
GSAAANRTID FVEPVESLIL SASPNPAAVN MSLTLCAELA GGSGVVYTWY
1760 1770 1780 1790 1800
LEEGLSWKTS MPSTTHTFAA PGLHLVRVTA ENQLGSVNAT VEVAIQVPVG
1810 1820 1830 1840 1850
GLSIRTSEPD SIFVAAGSTL PFWGQLAEGT NVTWCWTLPG GSKDSQYIAV
1860 1870 1880 1890 1900
RFSTAGSFSL QLNASNAVSW VSAMYNLTVE EPIVNLMLWA SSKVVAPGQP
1910 1920 1930 1940 1950
VHFEILLAAG SALTFRLQVG GSVPEVLPSP HFSHSFFRVG DHLVNVQAEN
1960 1970 1980 1990 2000
HVSHAQAQVR ILVLEAVVGL QVPNCCEPGM ATGTEKNFTA RVQRGSRVAY
2010 2020 2030 2040 2050
AWYFSLQKVQ GDSLVILSGR DVTYTPVAAG LLEIHVRAFN ELGGVNLTLM
2060 2070 2080 2090 2100
VEVQDIIQYV TLQSGRCFTN RSARFEAATS PSPRRVTYHW DFGDGTPVQK
2110 2120 2130 2140 2150
TEEFWADHYY LRPGDYHVEV NATNLVSFFV AQATVTVQVL ACREPEVEVA
2160 2170 2180 2190 2200
LPLQVLMRRS QRNYLEAHVD LRNCVSYQTE YRWEIYRTAS CQRPGRMAQM
2210 2220 2230 2240 2250
VLPGVDVSRP QLVVPRLALP VGHYCFVFVV SFGDTPLARS IQANVTVAAE
2260 2270 2280 2290 2300
RLVPIIEGGS YRVWSDTQDL VLDGSKSYDP NLEDGDQTPL NFHWACVAST
2310 2320 2330 2340 2350
QSETGGCVLN FGPRGSSVVT IPLERLEAGV EYTFNLIVWK AGRKEEATNQ
2360 2370 2380 2390 2400
TVLIRSGRVP IVSLECVSCK AQAVYEVSRS SYVYLEGHCH NCSRGYKQGC
2410 2420 2430 2440 2450
WAARTFSNKT LVLNETTTST GSTGMNLVVR PGALRDGEGY IFTLTVLGHS
2460 2470 2480 2490 2500
GEEEGCASIR LSPNRPPLGG SCRLFPLDSV RGLTTKVHFE CTGWRDAEDG
2510 2520 2530 2540 2550
GAPLVYALLL KRCRQSYCEN FCIYKGSLST YGAVLPPGFQ PLFVVSLAVV
2560 2570 2580 2590 2600
VQDQLGAAVV ALNRSLTIVL PEPSGNPADL VPWLHSLTAS VLPGLLKQAD
2610 2620 2630 2640 2650
PQHVIEYSLA LITVLNEYEQ APDVSEPNVE QQLRAQMRKN ITETLISLRV
2660 2670 2680 2690 2700
NTVDDIQQIT AALAQCMVSS RELMCRSCLK KMLQKLEGMM RILQAETTEG
2710 2720 2730 2740 2750
TLTPTTIADS ILNITGDLIH LASLDMQGPQ PLELGVEPPS LMVASKAYNL
2760 2770 2780 2790 2800
SSALMRILMR SRVLNEEPLT LAGEEIVALG KRSDPLSLLC YGKALGPSCH
2810 2820 2830 2840 2850
FSIPEAFSGA LSNLSDVVQL IFLVDSNPFP FGYISNYTVS TKVASMAFQT
2860 2870 2880 2890 2900
QTGTQIPIEQ LAAERAITVK VPNNSDQAAQ SSHNPVGSTI VQPQTSVSAV
2910 2920 2930 2940 2950
VTADNSNPQA GLHLRITYTV LNERYLSAEP EPYLAVYLHS VSQPNEYNCS
2960 2970 2980 2990 3000
ASRRISLEVL EGADHRLYTF FIAPGTGTLD RSYYLNLTSH FHWSALEVSV
3010 3020 3030 3040 3050
GLYTSLCQYF SEEMMMWRTE GIVPLEETSP SQAVCLTRHL TAFGASLFVP
3060 3070 3080 3090 3100
PSHVQFIFPE PSASINYIVL LTCVICLVTY VVMAMILRKL DQLDVSRVRV
3110 3120 3130 3140 3150
IPFCGKGGRF KYEILVKTGW SRGSGTTAHV GIMLYGEDNR SGHRHLDGDR
3160 3170 3180 3190 3200
AFHRNSLDIF QIATPHSLGS VWKIRVWHDN KGLSPAWFLQ HIIVRDLQSA
3210 3220 3230 3240 3250
RSTFFLVNDW LSVETEANGG LVEKEVLAAN EAALWQFQRL LVAELQRGFF
3260 3270 3280 3290 3300
DKHIWLSIWD RPPRSRFTRV QRVTCCVLLL CLFLAANAVW YGVVRDTTYS
3310 3320 3330 3340 3350
MGPVSSLISP GVDTVAIGLV SSVVVYPVYL AVLFLFRMSR SKVSGDQNPT
3360 3370 3380 3390 3400
PTGQQALDVD SYLDPSVLDS SLLTLSGLTE AFAGQVKNDL FLEDAKSLVC
3410 3420 3430 3440 3450
WPSSEGTLSW PDLLSDPSVV SSTLQRLTQG RPGCMLGSEE DGASLVSPSL
3460 3470 3480 3490 3500
PAKYLSASDE DLIHQVLADG ANNLVPTQDT LLETDLLTSL SSVPGEKTET
3510 3520 3530 3540 3550
LILQTVGEER PASMGLSWEQ SPVTRLSRTG LVEGFQKRLL PAWCAPLAHG
3560 3570 3580 3590 3600
LSLLLVAVAV AVSGWIGASF PPSVSVMWLL SSSSSFLASF LGWEPLKVLL
3610 3620 3630 3640 3650
EALYFSLVAK RLHPDEDDTL VESPAVTPVS ERVPRVRPPH GFALFLAKEE
3660 3670 3680 3690 3700
ARKVKRLHDM LKRLLVYMLF LLVTLLANYG DASCHGHAYR LQSAIKQELD
3710 3720 3730 3740 3750
SQAFLAITRS DEFWPWMSHV FLPYVHGNQS SPELGPPRLR QVRLQEAFCP
3760 3770 3780 3790 3800
DPSSSEHMCS AAGSLSTSDY GIGWQSVVQN GSETWAYSAP DLLGAWYWGY
3810 3820 3830 3840 3850
CAVYDSGGYI QELGLSLEES RARLGFLQLH NWLDSRSRAV FVELTRYSPA
3860 3870 3880 3890 3900
VGLHAAVTLR LEFPVAGHAL AAFSVRPFAL RRLSTGLSLP LLTSVCLLLF
3910 3920 3930 3940 3950
ALYFSMAEVQ TWRKDGCACT ARPDTWARCL LVILTAATGL VRLAQLGIAD
3960 3970 3980 3990 4000
RQWTHFVQDH PRHFTSFDQV AQLGSVARGL AASLLFLLLV KAAQQLRFVR
4010 4020 4030 4040 4050
QWSVFGKTLC RALPELMGAT LGLVLLGVAY AQMAILLISS GADTLYNMAR
4060 4070 4080 4090 4100
AFLVLCPGAR VPTLCPSESW YLSPLLCVGL WALRVWGALR LGAILLRWRY
4110 4120 4130 4140 4150
HALRGELYRP AWEPQDYEMV ELFLRRLRLW MGFSKVKEFR HKVRFEGMDP
4160 4170 4180 4190 4200
LPSRSSRGSK SSPVVLPPSS GSEASHPSTS SSQPDGPSAS LSRSTLKLEP
4210 4220 4230 4240 4250
EPSRLHAVFE SLLVQFDRLN QATEDVYQLE QQLQSLQGHG HNGPPSSPSP
4260 4270 4280 4290
GCFPGSQPAL PSRLSRASQG LDQTVGPNRV SLWPNNKVHP SST
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 ENSGT00700000104221.
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

Bgeei O08852.
ExpressionAtlasi O08852. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 117 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