Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Polycystin-1

Gene

Pkd1

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

Functioni

Involved in renal tubulogenesis (PubMed:24939912). Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:12514735). Acts as a regulator of cilium length, together with PKD2 (PubMed:20096584). 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.3 Publications

GO - Molecular functioni

  • calcium channel activity Source: BHF-UCL
  • carbohydrate binding Source: UniProtKB-KW
  • ion channel binding Source: MGI
  • protein domain specific binding Source: MGI
  • protein kinase binding Source: MGI

GO - Biological processi

  • blood vessel development Source: MGI
  • branching morphogenesis of an epithelial tube Source: UniProtKB
  • calcium ion transmembrane transport Source: BHF-UCL
  • calcium ion transport Source: MGI
  • cartilage condensation Source: MGI
  • cell cycle arrest Source: MGI
  • cytoplasmic sequestering of transcription factor Source: BHF-UCL
  • detection of mechanical stimulus Source: MGI
  • digestive tract development Source: Ensembl
  • embryonic placenta development Source: BHF-UCL
  • establishment of cell polarity Source: MGI
  • genitalia development Source: Ensembl
  • heart development Source: MGI
  • in utero embryonic development Source: MGI
  • JAK-STAT cascade Source: MGI
  • kidney development Source: BHF-UCL
  • liver development Source: MGI
  • lung epithelium development Source: Ensembl
  • lymph vessel morphogenesis Source: MGI
  • mesonephric duct development Source: Ensembl
  • metanephric ascending thin limb development Source: Ensembl
  • metanephric collecting duct development Source: Ensembl
  • metanephric distal tubule morphogenesis Source: Ensembl
  • metanephric proximal tubule development Source: Ensembl
  • neural tube development Source: Ensembl
  • nitrogen compound metabolic process Source: MGI
  • peptidyl-serine phosphorylation Source: UniProtKB
  • placenta blood vessel development Source: BHF-UCL
  • positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: MGI
  • positive regulation of cytosolic calcium ion concentration Source: Ensembl
  • positive regulation of protein binding Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein export from nucleus Source: UniProtKB
  • regulation of cell adhesion Source: MGI
  • regulation of mitotic spindle organization Source: MGI
  • regulation of proteasomal protein catabolic process Source: MGI
  • renal system development Source: MGI
  • response to fluid shear stress Source: MGI
  • single organismal cell-cell adhesion Source: MGI
  • skin development Source: Ensembl
  • spinal cord development Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiR-MMU-5620916. VxPx cargo-targeting to cilium.

Protein family/group databases

MEROPSiP02.038.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:97603. Pkd1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei3067 – 3087HelicalSequence analysisAdd BLAST21
Transmembranei3273 – 3293HelicalSequence analysisAdd BLAST21
Transmembranei3316 – 3336HelicalSequence analysisAdd BLAST21
Transmembranei3550 – 3570HelicalSequence analysisAdd BLAST21
Transmembranei3573 – 3593HelicalSequence analysisAdd BLAST21
Transmembranei3664 – 3684HelicalSequence analysisAdd BLAST21
Transmembranei3887 – 3907HelicalSequence analysisAdd BLAST21
Transmembranei3929 – 3949HelicalSequence analysisAdd BLAST21
Transmembranei3970 – 3990HelicalSequence analysisAdd BLAST21
Transmembranei4018 – 4038HelicalSequence analysisAdd BLAST21
Transmembranei4075 – 4095HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • basolateral plasma membrane Source: MGI
  • cell surface Source: UniProtKB
  • cilium Source: UniProtKB
  • cytoplasm Source: BHF-UCL
  • extracellular exosome Source: MGI
  • Golgi apparatus Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • lateral plasma membrane Source: Ensembl
  • motile cilium Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
  • polycystin complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000035405424 – 4293Polycystin-1Add BLAST4270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi50N-linked (GlcNAc...)Sequence analysis1
Glycosylationi89N-linked (GlcNAc...)Sequence analysis1
Glycosylationi116N-linked (GlcNAc...)Sequence analysis1
Glycosylationi121N-linked (GlcNAc...)Sequence analysis1
Glycosylationi187N-linked (GlcNAc...)Sequence analysis1
Glycosylationi239N-linked (GlcNAc...)Sequence analysis1
Glycosylationi370N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi436 ↔ 529By similarity
Disulfide bondi507 ↔ 521By similarity
Glycosylationi627N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi635 ↔ 648By similarity
Disulfide bondi642 ↔ 660By similarity
Glycosylationi662N-linked (GlcNAc...)Sequence analysis1
Glycosylationi740N-linked (GlcNAc...)Sequence analysis1
Glycosylationi804N-linked (GlcNAc...)Sequence analysis1
Glycosylationi835N-linked (GlcNAc...)Sequence analysis1
Glycosylationi848N-linked (GlcNAc...)Sequence analysis1
Glycosylationi859N-linked (GlcNAc...)Sequence analysis1
Glycosylationi884N-linked (GlcNAc...)Sequence analysis1
Glycosylationi915N-linked (GlcNAc...)Sequence analysis1
Glycosylationi998N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1004N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1028N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1084N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1096N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1107N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1172N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1188N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1234N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1263N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1330N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1342N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1376N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1444N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1449N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1468N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1535N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1548N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1557N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1643N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1657N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1706N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1730N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1788N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1831N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1863N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1876N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1987N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2046N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2070N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2121N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2244N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2349N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2391N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2408N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2414N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2563N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2640N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2713N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2749N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2813N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2836N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2873N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2948N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2986N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3139N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3728N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3780N-linked (GlcNAc...)Sequence analysis1
Modified residuei4156Phosphoserine; by PRKX; in vitroBy similarity1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei3040 – 3041Cleavage; by autolysisBy similarity2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO08852.
PaxDbiO08852.
PRIDEiO08852.

PTM databases

iPTMnetiO08852.
PhosphoSitePlusiO08852.

Expressioni

Gene expression databases

BgeeiENSMUSG00000032855.
GenevisibleiO08852. MM.

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) (PubMed:20856870). Interacts with PKD2L1 (PubMed:15548533). Interacts with BBS1, BBS4, BBS5 and TTC8. Interacts with RGS7 (By similarity).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202204. 3 interactors.
DIPiDIP-44233N.
IntActiO08852. 7 interactors.
MINTiMINT-5163387.
STRINGi10090.ENSMUSP00000049296.

Structurei

3D structure databases

ProteinModelPortaliO08852.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 67LRRNTAdd BLAST44
Repeati68 – 91LRR 1Add BLAST24
Repeati92 – 113LRR 2Add BLAST22
Domaini125 – 178LRRCTAdd BLAST54
Domaini177 – 271WSCPROSITE-ProRule annotationAdd BLAST95
Domaini272 – 359PKD 1PROSITE-ProRule annotationAdd BLAST88
Domaini415 – 530C-type lectinPROSITE-ProRule annotationAdd BLAST116
Domaini633 – 666LDL-receptor class A; atypicalAdd BLAST34
Domaini849 – 922PKD 2PROSITE-ProRule annotationAdd BLAST74
Domaini929 – 1014PKD 3PROSITE-ProRule annotationAdd BLAST86
Domaini1017 – 1123PKD 4PROSITE-ProRule annotationAdd BLAST107
Domaini1121 – 1209PKD 5PROSITE-ProRule annotationAdd BLAST89
Domaini1207 – 1292PKD 6PROSITE-ProRule annotationAdd BLAST86
Domaini1288 – 1377PKD 7PROSITE-ProRule annotationAdd BLAST90
Domaini1376 – 1463PKD 8PROSITE-ProRule annotationAdd BLAST88
Domaini1462 – 1545PKD 9PROSITE-ProRule annotationAdd BLAST84
Domaini1544 – 1629PKD 10PROSITE-ProRule annotationAdd BLAST86
Domaini1630 – 1718PKD 11PROSITE-ProRule annotationAdd BLAST89
Domaini1716 – 1802PKD 12PROSITE-ProRule annotationAdd BLAST87
Domaini1804 – 1886PKD 13PROSITE-ProRule annotationAdd BLAST83
Domaini1885 – 1970PKD 14PROSITE-ProRule annotationAdd BLAST86
Domaini1972 – 2053PKD 15PROSITE-ProRule annotationAdd BLAST82
Domaini2056 – 2144PKD 16PROSITE-ProRule annotationAdd BLAST89
Domaini2142 – 2828REJPROSITE-ProRule annotationAdd BLAST687
Domaini3004 – 3053GPSPROSITE-ProRule annotationAdd BLAST50
Domaini3110 – 3225PLATPROSITE-ProRule annotationAdd BLAST116

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili4210 – 4241Sequence analysisAdd BLAST32

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi3734 – 3746Polycystin motifAdd BLAST13

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi3581 – 3585Poly-Ser5
Compositional biasi4153 – 4194Ser-richAdd BLAST42

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

eggNOGiKOG3599. Eukaryota.
ENOG410XTGE. LUCA.
GeneTreeiENSGT00700000104221.
HOGENOMiHOG000168445.
HOVERGENiHBG049412.
InParanoidiO08852.
KOiK04985.
OMAiVSCKAQS.
OrthoDBiEOG091G004D.
TreeFamiTF316484.

Family and domain databases

Gene3Di2.60.40.670. 14 hits.
2.60.60.20. 1 hit.
3.10.100.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR016187. CTDL_fold.
IPR000483. Cys-rich_flank_reg_C.
IPR000203. GPS.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR000434. PC1.
IPR022409. PKD/Chitinase_dom.
IPR002859. PKD/REJ-like.
IPR013122. PKD1_2_channel.
IPR000601. PKD_dom.
IPR001024. PLAT/LH2_dom.
IPR006228. Polycystin_cat.
IPR014010. REJ_dom.
IPR002889. WSC_carb-bd.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
PF13855. LRR_8. 1 hit.
PF00801. PKD. 14 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.
SSF52058. SSF52058. 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

« Hide

        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)DescriptionActionsGraphical viewLength
Sequence conflicti3L → P in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti771R → Q in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti871E → D in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti1180A → T in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti1292H → R in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti1632A → V in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti1684S → A in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti1770A → T in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti2085R → C in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti2507A → V in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti3956F → C in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti3962R → H in AAC53207 (PubMed:9107672).Curated1
Sequence conflicti4237Q → R in AAC53207 (PubMed:9107672).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliO08852.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202204. 3 interactors.
DIPiDIP-44233N.
IntActiO08852. 7 interactors.
MINTiMINT-5163387.
STRINGi10090.ENSMUSP00000049296.

Protein family/group databases

MEROPSiP02.038.

PTM databases

iPTMnetiO08852.
PhosphoSitePlusiO08852.

Proteomic databases

MaxQBiO08852.
PaxDbiO08852.
PRIDEiO08852.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5310.
MGIiMGI:97603. Pkd1.

Phylogenomic databases

eggNOGiKOG3599. Eukaryota.
ENOG410XTGE. LUCA.
GeneTreeiENSGT00700000104221.
HOGENOMiHOG000168445.
HOVERGENiHBG049412.
InParanoidiO08852.
KOiK04985.
OMAiVSCKAQS.
OrthoDBiEOG091G004D.
TreeFamiTF316484.

Enzyme and pathway databases

ReactomeiR-MMU-5620916. VxPx cargo-targeting to cilium.

Miscellaneous databases

ChiTaRSiPkd1. mouse.
PROiO08852.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032855.
GenevisibleiO08852. MM.

Family and domain databases

Gene3Di2.60.40.670. 14 hits.
2.60.60.20. 1 hit.
3.10.100.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR016187. CTDL_fold.
IPR000483. Cys-rich_flank_reg_C.
IPR000203. GPS.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR000434. PC1.
IPR022409. PKD/Chitinase_dom.
IPR002859. PKD/REJ-like.
IPR013122. PKD1_2_channel.
IPR000601. PKD_dom.
IPR001024. PLAT/LH2_dom.
IPR006228. Polycystin_cat.
IPR014010. REJ_dom.
IPR002889. WSC_carb-bd.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
PF13855. LRR_8. 1 hit.
PF00801. PKD. 14 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.
SSF52058. SSF52058. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 137 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

Similar proteinsi

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