PKD1_HUMAN
ID PKD1_HUMAN Reviewed; 4303 AA.
AC P98161; Q15140; Q15141;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 251.
DE RecName: Full=Polycystin-1 {ECO:0000305};
DE Short=PC1;
DE AltName: Full=Autosomal dominant polycystic kidney disease 1 protein;
DE Flags: Precursor;
GN Name=PKD1 {ECO:0000312|HGNC:HGNC:9008};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-1092.
RX PubMed=7736581; DOI=10.1016/0092-8674(95)90339-9;
RA Gluecksmann-Kuis M.A., Tayber O., Woolf E.A., Bougueleret L., Deng N.,
RA Alperin G.D., Iris F., Hawkins F., Munro C., Lakey N., Duyk G.,
RA Schneider M.C., Geng L., Zhang F., Zhao Z., Torosian S., Reeders S.T.,
RA Bork P., Pohlschmidt M., Loehning C., Kraus B., Nowicka U., Leung A.L.S.,
RA Frischauf A.-M.;
RT "Polycystic kidney disease: the complete structure of the PKD1 gene and its
RT protein.";
RL Cell 81:289-298(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP GLN-739.
RX PubMed=7663510; DOI=10.1038/ng0695-151;
RA Hughes J., Ward C.J., Peral B., Aspinwall R., Clark K., San Millan J.L.,
RA Gamble V., Harris P.C.;
RT "The polycystic kidney disease 1 (PKD1) gene encodes a novel protein with
RT multiple cell recognition domains.";
RL Nat. Genet. 10:151-160(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2769-4303.
RX PubMed=8004675; DOI=10.1016/0092-8674(94)90137-6;
RA Ward C.J., Peral B., Hughes J., Thomas S., Gamble V., Maccarthy A.B.,
RA Sloane-Stanley J., Buckle V.J., Kearney L., Higgs D.R., Ratcliffe P.J.,
RA Harris P.C., Roelfsema J.H., Spruit L.L., Saris J.J., Dauwerse H.G.,
RA Peters D.J.M., Breuning M.H., Nellist M., Brook-Carter P.T.,
RA Maheshwar M.M., Cordeiro I., Santos H., Cabral P., Sampson J.R.,
RA Janssen B., Hesseling-Janssen A.L.W., van den Ouweland A.M.W., Eussen B.,
RA Verhoef S., Lindhout D., Halley D.J.J.;
RT "The polycystic kidney disease 1 gene encodes a 14 kb transcript and lies
RT within a duplicated region on chromosome 16.";
RL Cell 77:881-894(1994).
RN [5]
RP ERRATUM OF PUBMED:8004675.
RX PubMed=8069919;
RA Ward C.J., Peral B., Hughes J., Thomas S., Gamble V., Maccarthy A.B.,
RA Sloane-Stanley J., Buckle V.J., Kearney L., Higgs D.R., Ratcliffe P.J.,
RA Harris P.C., Roelfsema J.H., Spruit L.L., Saris J.J., Dauwerse H.G.,
RA Peters D.J.M., Breuning M.H., Nellist M., Brook-Carter P.T.,
RA Maheshwar M.M., Cordeiro I., Santos H., Cabral P., Sampson J.R.,
RA Janssen B., Hesseling-Janssen A.L.W., van den Ouweland A.M.W., Eussen B.,
RA Verhoef S., Lindhout D., Halley D.J.J.;
RL Cell 78:725-725(1994).
RN [6]
RP INTERACTION WITH RGS7, AND SUBCELLULAR LOCATION.
RX PubMed=10339594; DOI=10.1073/pnas.96.11.6371;
RA Kim E., Arnould T., Sellin L., Benzing T., Comella N., Kocher O.,
RA Tsiokas L., Sukhatme V.P., Walz G.;
RT "Interaction between RGS7 and polycystin.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6371-6376(1999).
RN [7]
RP FUNCTION IN RENAL TUBULOGENESIS, AUTOCATALYTIC CLEAVAGE AT LEU-3048,
RP CHARACTERIZATION OF VARIANTS PKD1 LYS-2771; PRO-2921; PRO-2993 AND
RP ARG-3016, AND CHARACTERIZATION OF VARIANT GLN-2791.
RX PubMed=12482949; DOI=10.1073/pnas.252484899;
RA Qian F., Boletta A., Bhunia A.K., Xu H., Liu L., Ahrabi A.K., Watnick T.J.,
RA Zhou F., Germino G.G.;
RT "Cleavage of polycystin-1 requires the receptor for egg jelly domain and is
RT disrupted by human autosomal-dominant polycystic kidney disease 1-
RT associated mutations.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16981-16986(2002).
RN [8]
RP AUTOCATALYTIC CLEAVAGE AT LEU-3048, AND MUTAGENESIS OF THR-3049.
RX PubMed=17525154; DOI=10.1074/jbc.m703218200;
RA Wei W., Hackmann K., Xu H., Germino G., Qian F.;
RT "Characterization of cis-autoproteolysis of polycystin-1, the product of
RT human polycystic kidney disease 1 gene.";
RL J. Biol. Chem. 282:21729-21737(2007).
RN [9]
RP PHOSPHORYLATION AT SER-4166, AND INTERACTION WITH PRKX.
RX PubMed=17980165; DOI=10.1016/j.bbadis.2007.09.003;
RA Li X., Burrow C.R., Polgar K., Hyink D.P., Gusella G.L., Wilson P.D.;
RT "Protein kinase X (PRKX) can rescue the effects of polycystic kidney
RT disease-1 gene (PKD1) deficiency.";
RL Biochim. Biophys. Acta 1782:1-9(2008).
RN [10]
RP INTERACTION WITH PKD2.
RX PubMed=20881056; DOI=10.1091/mbc.e10-04-0377;
RA Streets A.J., Needham A.J., Gill S.K., Ong A.C.;
RT "Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is
RT essential for its effects on cell growth and calcium channel activity.";
RL Mol. Biol. Cell 21:3853-3865(2010).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=20980620; DOI=10.1091/mbc.e10-05-0407;
RA Chapin H.C., Rajendran V., Caplan M.J.;
RT "Polycystin-1 surface localization is stimulated by polycystin-2 and
RT cleavage at the G protein-coupled receptor proteolytic site.";
RL Mol. Biol. Cell 21:4338-4348(2010).
RN [12]
RP INTERACTION WITH NPHP1.
RX PubMed=20856870; DOI=10.1371/journal.pone.0012719;
RA Wodarczyk C., Distefano G., Rowe I., Gaetani M., Bricoli B., Muorah M.,
RA Spitaleri A., Mannella V., Ricchiuto P., Pema M., Castelli M.,
RA Casanova A.E., Mollica L., Banzi M., Boca M., Antignac C., Saunier S.,
RA Musco G., Boletta A.;
RT "Nephrocystin-1 forms a complex with polycystin-1 via a polyproline
RT motif/SH3 domain interaction and regulates the apoptotic response in
RT mammals.";
RL PLoS ONE 5:E12719-E12719(2010).
RN [13]
RP INTERACTION WITH BBS1; BBS4; BBS5 AND TTC8.
RX PubMed=24939912; DOI=10.1093/hmg/ddu267;
RA Su X., Driscoll K., Yao G., Raed A., Wu M., Beales P.L., Zhou J.;
RT "Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary trafficking of
RT polycystic kidney disease 1 protein.";
RL Hum. Mol. Genet. 23:5441-5451(2014).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=27259053; DOI=10.1016/j.ajhg.2016.05.004;
RG Genkyst Study Group, HALT Progression of Polycystic Kidney Disease Group;
RG Consortium for Radiologic Imaging Studies of Polycystic Kidney Disease;
RA Porath B., Gainullin V.G., Cornec-Le Gall E., Dillinger E.K., Heyer C.M.,
RA Hopp K., Edwards M.E., Madsen C.D., Mauritz S.R., Banks C.J., Baheti S.,
RA Reddy B., Herrero J.I., Banales J.M., Hogan M.C., Tasic V., Watnick T.J.,
RA Chapman A.B., Vigneau C., Lavainne F., Audrezet M.P., Ferec C., Le Meur Y.,
RA Torres V.E., Harris P.C.;
RT "Mutations in GANAB, encoding the glucosidase IIalpha subunit, cause
RT autosomal-dominant polycystic kidney and liver disease.";
RL Am. J. Hum. Genet. 98:1193-1207(2016).
RN [15]
RP FUNCTION, INTERACTION WITH DVL1; DVL2; WNT3A; WNT4; WNT5A AND WNT9B,
RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT ILE-99.
RX PubMed=27214281; DOI=10.1038/ncb3363;
RA Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J.,
RA Maskey D., Watnick T., Wessely O., Tsiokas L.;
RT "The polycystin complex mediates Wnt/Ca(2+) signalling.";
RL Nat. Cell Biol. 18:752-764(2016).
RN [16]
RP STRUCTURE BY NMR OF 275-354.
RX PubMed=9889186; DOI=10.1093/emboj/18.2.297;
RA Bycroft M., Bateman A., Clarke J., Hamill S.J., Sandford R., Thomas R.L.,
RA Chothia C.;
RT "The structure of a PKD domain from polycystin-1: implications for
RT polycystic kidney disease.";
RL EMBO J. 18:297-305(1999).
RN [17] {ECO:0007744|PDB:6A70}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 3049-4169 IN COMPLEX
RP WITH PKD2, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=30093605; DOI=10.1126/science.aat9819;
RA Su Q., Hu F., Ge X., Lei J., Yu S., Wang T., Zhou Q., Mei C., Shi Y.;
RT "Structure of the human PKD1-PKD2 complex.";
RL Science 361:0-0(2018).
RN [18]
RP REVIEW.
RX PubMed=11698076; DOI=10.1016/s0165-6147(00)01832-0;
RA Stayner C., Zhou J.;
RT "Polycystin channels and kidney disease.";
RL Trends Pharmacol. Sci. 22:543-546(2001).
RN [19]
RP VARIANT PKD1 3748-ARG--VAL-3752 DEL, AND VARIANT ASP-3632.
RX PubMed=8554072;
RA Peral B., San Millan J.L., Ong A.C.M., Gamble V., Ward C.J., Strong C.,
RA Harris P.C.;
RT "Screening the 3' region of the polycystic kidney disease 1 (PKD1) gene
RT reveals six novel mutations.";
RL Am. J. Hum. Genet. 58:86-96(1996).
RN [20]
RP VARIANTS PKD1 PRO-2993; ARG-3016 AND VAL-3511, AND VARIANTS MET-3510 AND
RP PHE-4190.
RX PubMed=9199561; DOI=10.1086/515467;
RA Peral B., Gamble V., Strong C., Ong A.C.M., Sloane-Stanley J., Zerres K.,
RA Winearls C.G., Harris P.C.;
RT "Identification of mutations in the duplicated region of the polycystic
RT kidney disease 1 gene (PKD1) by a novel approach.";
RL Am. J. Hum. Genet. 60:1399-1410(1997).
RN [21]
RP VARIANT ALA-4058.
RX PubMed=9150733; DOI=10.1007/s004390050421;
RA Constantinides R., Xenophontos S.L., Neophytou P., Nomura S., Pierides A.,
RA Constantinou-Deltas C.D.;
RT "New amino acid polymorphism, Ala/Val4058, in exon 45 of the polycystic
RT kidney disease 1 gene: evolution of alleles.";
RL Hum. Genet. 99:644-647(1997).
RN [22]
RP VARIANTS PKD1 VAL-2763; THR-2826 AND LEU-3008, AND VARIANTS THR-2760;
RP PRO-2761; THR-2764; GLN-2791 AND LEU-3066.
RX PubMed=9285784; DOI=10.1093/hmg/6.9.1473;
RA Watnick T.J., Piontek K.B., Cordal T.M., Weber H., Gandolph M.A., Qian F.,
RA Lens X.M., Neumann H.P.H., Germino G.G.;
RT "An unusual pattern of mutation in the duplicated portion of PKD1 is
RT revealed by use of a novel strategy for mutation detection.";
RL Hum. Mol. Genet. 6:1473-1481(1997).
RN [23]
RP VARIANT PKD1 THR-3678.
RX PubMed=9259200;
RX DOI=10.1002/(sici)1098-1004(1997)10:2<164::aid-humu9>3.0.co;2-k;
RA Turco A.E., Rossetti S., Bresin E., Englisch S., Corra S., Pignatti P.F.;
RT "Three novel mutations of the PKD1 gene in Italian families with autosomal
RT dominant polycystic kidney disease.";
RL Hum. Mutat. 10:164-167(1997).
RN [24]
RP VARIANT PKD1 ASP-4032, AND VARIANT VAL-4045.
RX PubMed=9521593; DOI=10.1007/s004390050681;
RA Daniells C., Maheshwar M.M., Lazarou L., Davies F., Coles G., Ravine D.;
RT "Novel and recurrent mutations in the PKD1 (polycystic kidney disease)
RT gene.";
RL Hum. Genet. 102:216-220(1998).
RN [25]
RP VARIANT PKD1 MET-3375.
RX PubMed=9921908; DOI=10.1007/s004390050896;
RA Koptides M., Constantinides R., Kyriakides G., Hadjigavriel M.,
RA Patsalis P.C., Pierides A., Deltas C.C.;
RT "Loss of heterozygosity in polycystic kidney disease with a missense
RT mutation in the repeated region of PKD1.";
RL Hum. Genet. 103:709-717(1998).
RN [26]
RP VARIANTS PKD1 LEU-324 AND SER-845, AND VARIANTS ARG-1399 AND LEU-1786.
RX PubMed=10364515; DOI=10.1086/302460;
RA Thomas R.L., McConnell R., Whittacker J., Kirkpatrick P., Bradley J.,
RA Sandford R.;
RT "Identification of mutations in the repeated part of the autosomal dominant
RT polycystic kidney disease type 1 gene, PKD1, by long-range PCR.";
RL Am. J. Hum. Genet. 65:39-49(1999).
RN [27]
RP VARIANTS PKD1 PRO-2392 AND PHE-2423, AND VARIANTS ARG-1399; GLN-2548 AND
RP ARG-2638.
RX PubMed=10577909; DOI=10.1086/302657;
RA Watnick T., Phakdeekitcharoen B., Johnson A., Gandolph M.A., Wang M.,
RA Briefel G., Klinger K.W., Kimberling W., Gabow P., Germino G.G.;
RT "Mutation detection of PKD1 identifies a novel mutation common to three
RT families with aneurysms and/or very-early-onset disease.";
RL Am. J. Hum. Genet. 65:1561-1571(1999).
RN [28]
RP VARIANTS PKD1 LEU-LEU-PHE-3996 INS; GLY-4136 AND CYS-4154, AND VARIANTS.
RX PubMed=10987650; DOI=10.1007/s004390051094;
RA Perrichot R.A., Mercier B., Simon P.M., Whebe B., Cledes J., Ferec C.;
RT "DGGE screening of PKD1 gene reveals novel mutations in a large cohort of
RT 146 unrelated patients.";
RL Hum. Genet. 105:231-239(1999).
RN [29]
RP VARIANTS PKD1 3748-ARG--VAL-3752 DEL AND LEU-4132 DEL, AND VARIANT
RP VAL-4045.
RX PubMed=10647901; DOI=10.1007/s004399900177;
RA Afzal A.R., Hand M., Ternes-Pereira E., Saggar-Malik A., Taylor R.,
RA Jeffery S.;
RT "Novel mutations in the 3 region of the polycystic kidney disease 1 (PKD1)
RT gene.";
RL Hum. Genet. 105:648-653(1999).
RN [30]
RP VARIANTS PKD1 PRO-4225 AND TRP-4276.
RX PubMed=10200984; DOI=10.1046/j.1523-1755.1999.00368.x;
RA Badenas C., Torra R., San Millan J.L., Lucero L., Mila M., Estivill X.,
RA Darnell A.;
RT "Mutational analysis within the 3' region of the PKD1 gene.";
RL Kidney Int. 55:1225-1233(1999).
RN [31]
RP VARIANTS PKD1 MET-2250; TRP-2329 AND CYS-2379, AND VARIANTS LEU-3066;
RP VAL-3139 AND LEU-3193.
RX PubMed=10854095; DOI=10.1038/sj.ejhg.5200459;
RA Perrichot R., Mercier B., Quere I., Carre A., Simon P., Whebe B.,
RA Cledes J., Ferec C.;
RT "Novel mutations in the duplicated region of PKD1 gene.";
RL Eur. J. Hum. Genet. 8:353-359(2000).
RN [32]
RP VARIANTS PKD1 HIS-3247 AND MET-3382.
RX PubMed=11216660; DOI=10.1089/109065700750065108;
RA Afzal A.R., Florencio R.N., Taylor R., Patton M.A., Saggar-Malik A.,
RA Jeffery S.;
RT "Novel mutations in the duplicated region of the polycystic kidney disease
RT 1 (PKD1) gene provides supporting evidence for gene conversion.";
RL Genet. Test. 4:365-370(2000).
RN [33]
RP VARIANTS PKD1 PRO-2921 AND MET-3375, AND VARIANT LEU-3066.
RX PubMed=10923040;
RX DOI=10.1002/1098-1004(200008)16:2<176::aid-humu11>3.0.co;2-h;
RA Koptides M., Mean R., Demetriou K., Constantinides R., Pierides A.,
RA Harris P.C., Deltas C.C.;
RT "Screening of the PKD1 duplicated region reveals multiple single nucleotide
RT polymorphisms and a de novo mutation in Hellenic polycystic kidney disease
RT families.";
RL Hum. Mutat. 16:176-176(2000).
RN [34]
RP VARIANTS PKD1 GLN-3719 AND PRO-3852, AND VARIANT VAL-4045.
RX PubMed=11058904;
RX DOI=10.1002/1098-1004(200011)16:5<444::aid-humu11>3.0.co;2-c;
RA Aguiari G., Savelli S., Garbo M., Bozza A., Augello G., Penolazzi L.,
RA De Paoli Vitali E., La Torre C., Cappelli G., Piva R., del Senno L.;
RT "Novel splicing and missense mutations in autosomal dominant polycystic
RT kidney disease 1 (PKD1) gene: expression of mutated genes.";
RL Hum. Mutat. 16:444-445(2000).
RN [35]
RP VARIANTS PKD1 SER-1166; GLU-1956; CYS-2408 AND GLY-2442--2443 INS, AND
RP VARIANTS HIS-1995 AND ASN-2604.
RX PubMed=11012875; DOI=10.1046/j.1523-1755.2000.00302.x;
RA Phakdeekitcharoen B., Watnick T.J., Ahn C., Whang D.-Y., Burkhart B.,
RA Germino G.G.;
RT "Thirteen novel mutations of the replicated region of PKD1 in an Asian
RT population.";
RL Kidney Int. 58:1400-1412(2000).
RN [36]
RP VARIANTS PKD1 TRP-3753 AND ASN-3815.
RX PubMed=10729710; DOI=10.1016/s1383-5726(99)00013-8;
RA Kim U.K., Jin D.K., Ahn C., Shin J.H., Lee K.B., Kim S.H., Chae J.J.,
RA Hwang D.Y., Lee J.G., Namkoong Y., Lee C.C.;
RT "Novel mutations of the PKD1 gene in Korean patients with autosomal
RT dominant polycystic kidney disease.";
RL Mutat. Res. 432:39-45(2000).
RN [37]
RP VARIANTS PKD1 GLN-13; PHE-75; CYS-139; 1992-PHE-THR-1993 DELINS LEU;
RP 2220-ARG--PRO-2224 DEL; ASP-2336; ASP-2752; ILE-LEU-MET-ARG-2765 INS;
RP MET-2768; LYS-2771; PRO-2816; SER-2858; 3012-THR--TYR-3017 DEL AND
RP 3748-LEU--ARG-3752 DEL, AND VARIANTS SER-2674; MET-2708; THR-2734;
RP LEU-2735; CYS-2765; MET-2782; ARG-2814; GLY-2888; ILE-2905; ASP-2966 AND
RP LEU-3066.
RX PubMed=11115377; DOI=10.1086/316939;
RA Rossetti S., Strmecki L., Gamble V., Burton S., Sneddon V., Peral B.,
RA Roy S., Bakkaloglu A., Komel R., Winearls C.G., Harris P.C.;
RT "Mutation analysis of the entire PKD1 gene: genetic and diagnostic
RT implications.";
RL Am. J. Hum. Genet. 68:46-63(2001).
RN [38]
RP VARIANTS PKD1 LEU-2471; LEU-2519; GLY-2579 DEL; LEU-2613 DEL; ILE-2649 AND
RP PHE-2978 DEL, AND VARIANTS MET-2582; ARG-2638; ASN-2972 AND LEU-3066.
RX PubMed=11571556; DOI=10.1038/sj.ejhg.5200696;
RA Bouba I., Koptides M., Mean R., Costi C.-E., Demetriou K., Georgiou I.,
RA Pierides A., Siamopoulos K., Deltas C.C.;
RT "Novel PKD1 deletions and missense variants in a cohort of Hellenic
RT polycystic kidney disease families.";
RL Eur. J. Hum. Genet. 9:677-684(2001).
RN [39]
RP VARIANTS PKD1 ARG-967; ARG-2696; GLY-2985; CYS-3039 AND ILE-3285, AND
RP VARIANTS VAL-88 AND ARG-3311.
RX PubMed=11316854; DOI=10.1681/asn.v125955;
RA Phakdeekitcharoen B., Watnick T.J., Germino G.G.;
RT "Mutation analysis of the entire replicated portion of PKD1 using genomic
RT DNA samples.";
RL J. Am. Soc. Nephrol. 12:955-963(2001).
RN [40]
RP INVOLVEMENT IN PKD1, AND VARIANTS MET-3008 AND MET-3510.
RX PubMed=11558899; DOI=10.1007/s100380170032;
RA Mizoguchi M., Tamura T., Yamaki A., Higashihara E., Shimizu Y.;
RT "Mutations of the PKD1 gene among Japanese autosomal dominant polycystic
RT kidney disease patients, including one heterozygous mutation identified in
RT members of the same family.";
RL J. Hum. Genet. 46:511-517(2001).
RN [41]
RP VARIANTS PKD1 ARG-3560; GLN-3719 AND TRP-3753, AND VARIANT MET-3510.
RX PubMed=11691639; DOI=10.1016/s0027-5107(01)00226-3;
RA Tsuchiya K., Komeda M., Takahashi M., Yamashita N., Cigira M., Suzuki T.,
RA Suzuki K., Nihei H., Mochizuki T.;
RT "Mutational analysis within the 3' region of the PKD1 gene in Japanese
RT families.";
RL Mutat. Res. 458:77-84(2001).
RN [42]
RP VARIANTS PKD1 SER-3602 AND SER-4255.
RX PubMed=12220456; DOI=10.1034/j.1399-0004.2002.620211.x;
RA Eo H.-S., Lee J.G., Ahn C., Cho J.T., Hwang D.Y., Hwang Y.H., Lee E.J.,
RA Kim Y.S., Han J.S., Kim S., Lee J.S., Jeoung D.I., Lee S.E., Kim U.K.;
RT "Three novel mutations of the PKD1 gene in Korean patients with autosomal
RT dominant polycystic kidney disease.";
RL Clin. Genet. 62:169-174(2002).
RN [43]
RP VARIANTS PKD1 CYS-381; ASP-2185; THR-2421 DEL; ASP-2785 AND
RP 3027-THR--ARG-3039 DEL, AND VARIANTS GLN-739; THR-1092; ARG-1399; MET-1649;
RP ARG-2638; CYS-2765 AND LEU-3066.
RX PubMed=11857740; DOI=10.1002/humu.10045;
RA McCluskey M., Schiavello T., Hunter M., Hantke J., Angelicheva D.,
RA Bogdanova N., Markoff A., Thomas M., Dworniczak B., Horst J.,
RA Kalaydjieva L.;
RT "Mutation detection in the duplicated region of the polycystic kidney
RT disease 1 (PKD1) gene in PKD1-linked Australian families.";
RL Hum. Mutat. 19:240-250(2002).
RN [44]
RP VARIANTS PKD1 ILE-2083; ARG-2814 AND PRO-2816, AND VARIANTS MET-87 AND
RP MET-3510.
RX PubMed=12007219; DOI=10.1002/humu.10080;
RA Inoue S., Inoue K., Utsunomiya M., Nozaki J., Yamada Y., Iwasa T., Mori E.,
RA Yoshinaga T., Koizumi A.;
RT "Mutation analysis in PKD1 of Japanese autosomal dominant polycystic kidney
RT disease patients.";
RL Hum. Mutat. 19:622-628(2002).
RN [45]
RP VARIANT PKD1 HIS-987, AND VARIANTS ARG-1399 AND VAL-4045.
RX PubMed=12070253; DOI=10.1136/jmg.39.6.422;
RA Burtey S., Lossi A.M., Bayle J., Berland Y., Fontes M.;
RT "Mutation screening of the PKD1 transcript by RT-PCR.";
RL J. Med. Genet. 39:422-429(2002).
RN [46]
RP VARIANTS PKD1 TRP-1340; LYS-1811; CYS-2092; ILE-2260 DEL; PHE-3167 AND
RP PRO-3852, AND VARIANTS LEU-61; SER-572; THR-1092; SER-1168; ARG-1399;
RP LEU-1684; ILE-1943; ARG-2638; SER-2674; MET-2708; ARG-2814; LEU-2958;
RP ASN-2977; MET-3057; GLN-3435; VAL-3512; VAL-4045; VAL-4059; SER-4124;
RP ILE-4146 AND PHE-4190.
RX PubMed=11967008; DOI=10.1046/j.1523-1755.2002.00326.x;
RA Rossetti S., Chauveau D., Walker D., Saggar-Malik A., Winearls C.G.,
RA Torres V.E., Harris P.C.;
RT "A complete mutation screen of the ADPKD genes by DHPLC.";
RL Kidney Int. 61:1588-1599(2002).
RN [47]
RP VARIANTS PKD1 ASP-3632; LEU-3649 AND THR-3678, AND VARIANTS VAL-4045;
RP VAL-4059; GLU-4102; PRO-4106 AND ILE-4146.
RX PubMed=11773467; DOI=10.1093/ndt/17.1.75;
RA Ding L., Zhang S., Qiu W., Xiao C., Wu S., Zhang G., Cheng L., Zhang S.;
RT "Novel mutations of PKD1 gene in Chinese patients with autosomal dominant
RT polycystic kidney disease.";
RL Nephrol. Dial. Transplant. 17:75-80(2002).
RN [48]
RP VARIANTS PKD1 ARG-164; GLY-210; ARG-508; ASP-690; ASN-1240 DEL; PRO-1667;
RP LYS-1811; CYS-2092; CYS-2200; ILE-2260 DEL; ARG-2370; TYR-2373; LYS-2771;
RP LEU-2802; ASN-3188 DEL; LEU-3355; PRO-3682 AND ARG-3751.
RX PubMed=12842373; DOI=10.1016/s0140-6736(03)13773-7;
RA Rossetti S., Chauveau D., Kubly V., Slezak J.M., Saggar-Malik A.K., Pei Y.,
RA Ong A.C.M., Stewart F., Watson M.L., Bergstralh E.J., Winearls C.G.,
RA Torres V.E., Harris P.C.;
RT "Association of mutation position in polycystic kidney disease 1 (PKD1)
RT gene and development of a vascular phenotype.";
RL Lancet 361:2196-2201(2003).
RN [49]
RP VARIANTS PKD1 SER-845; MET-3138 AND PRO-3954, AND VARIANTS HIS-36;
RP ARG-2638; LEU-3066; MET-3510; VAL-3512; VAL-4045 AND VAL-4059.
RX PubMed=15772804; DOI=10.1007/s00109-005-0644-6;
RA Peltola P., Lumiaho A., Miettinen R., Pihlajamaeki J., Sandford R.,
RA Laakso M.;
RT "Genetics and phenotypic characteristics of autosomal dominant polycystic
RT kidney disease in Finns.";
RL J. Mol. Med. 83:638-646(2005).
RN [50]
RP VARIANTS PKD1 LEU-61; ILE-99; TYR-594; MET-1242; CYS-2200; LYS-2422;
RP ARG-2638; LEU-3066; SER-3726 AND VAL-4155, AND VARIANTS HIS-36; GLN-739;
RP THR-1092; ARG-1399; THR-1516; THR-1871; VAL-1926; ASP-1952; MET-2708;
RP ARG-2814; VAL-3512; VAL-4045 AND VAL-4059.
RX PubMed=18837007; DOI=10.1002/humu.20842;
RA Tan Y.-C., Blumenfeld J.D., Anghel R., Donahue S., Belenkaya R., Balina M.,
RA Parker T., Levine D., Leonard D.G.B., Rennert H.;
RT "Novel method for genomic analysis of PKD1 and PKD2 mutations in autosomal
RT dominant polycystic kidney disease.";
RL Hum. Mutat. 30:264-273(2009).
RN [51]
RP VARIANTS PKD1 GLY-97; ARG-436; PRO-442; ARG-727; PRO-727; ASP-2391;
RP TRP-2434; TYR-2546; CYS-2569; THR-2646; ARG-2889; PRO-3154; ARG-3603 AND
RP GLN-3750.
RX PubMed=21115670; DOI=10.1093/ndt/gfq720;
RA Hoefele J., Mayer K., Scholz M., Klein H.G.;
RT "Novel PKD1 and PKD2 mutations in autosomal dominant polycystic kidney
RT disease (ADPKD).";
RL Nephrol. Dial. Transplant. 26:2181-2188(2011).
RN [52]
RP VARIANTS PKD1 CYS-325; TRP-611; ASP-698; PRO-727; GLY-1206; CYS-2379;
RP CYS-2767; LYS-2771; ARG-2995; SER-3651; GLN-3750; TRP-3753; CYS-4150 AND
RP TRP-4276.
RX PubMed=22508176; DOI=10.1002/humu.22103;
RA Audrezet M.P., Gall E.C., Chen J.M., Redon S., Quere I., Creff J.,
RA Benech C., Maestri S., Meur Y.L., Ferec C.;
RT "Autosomal dominant polycystic kidney disease: Comprehensive mutation
RT analysis of PKD1 and PKD2 in 700 unrelated patients.";
RL Hum. Mutat. 33:1239-1250(2012).
CC -!- FUNCTION: Component of a heteromeric calcium-permeable ion channel
CC formed by PKD1 and PKD2 that is activated by interaction between PKD1
CC and a Wnt family member, such as WNT3A and WNT9B (PubMed:27214281).
CC Both PKD1 and PKD2 are required for channel activity (PubMed:27214281).
CC Involved in renal tubulogenesis (PubMed:12482949). Involved in fluid-
CC flow mechanosensation by the primary cilium in renal epithelium (By
CC similarity). Acts as a regulator of cilium length, together with PKD2
CC (By similarity). The dynamic control of cilium length is essential in
CC the regulation of mechanotransductive signaling (By similarity). The
CC cilium length response creates a negative feedback loop whereby fluid
CC shear-mediated deflection of the primary cilium, which decreases
CC intracellular cAMP, leads to cilium shortening and thus decreases flow-
CC induced signaling (By similarity). May be an ion-channel regulator.
CC Involved in adhesive protein-protein and protein-carbohydrate
CC interactions. {ECO:0000250|UniProtKB:O08852,
CC ECO:0000269|PubMed:12482949, ECO:0000269|PubMed:27214281}.
CC -!- SUBUNIT: Interacts with PKD2; the interaction is required for ciliary
CC localization (PubMed:20881056). Component of a heterotetrameric channel
CC complex with PKD2; the tetramer contains one PKD1 chain and three PKD2
CC chains (PubMed:30093605). Interacts with PKD2L1 (By similarity).
CC Interacts with PRKX; involved in differentiation and controlled
CC morphogenesis of the kidney (PubMed:17980165). Interacts (via
CC extracellular domain) with WNT3A, WNT4, WNT5A and WNT9B
CC (PubMed:27214281). Interacts with DVL1 and DVL2 (PubMed:27214281).
CC Interacts with NPHP1 (via SH3 domain) (PubMed:20856870). Interacts with
CC BBS1, BBS4, BBS5 and TTC8 (PubMed:24939912). Interacts with RGS7
CC (PubMed:10339594). {ECO:0000250|UniProtKB:O08852,
CC ECO:0000269|PubMed:10339594, ECO:0000269|PubMed:17980165,
CC ECO:0000269|PubMed:20856870, ECO:0000269|PubMed:20881056,
CC ECO:0000269|PubMed:24939912, ECO:0000269|PubMed:27214281,
CC ECO:0000269|PubMed:30093605}.
CC -!- INTERACTION:
CC P98161; O15259: NPHP1; NbExp=2; IntAct=EBI-1752013, EBI-953828;
CC P98161; Q13563: PKD2; NbExp=8; IntAct=EBI-1752013, EBI-7813714;
CC P98161; Q13563-1: PKD2; NbExp=5; IntAct=EBI-1752013, EBI-9837017;
CC P98161-1; Q13563: PKD2; NbExp=4; IntAct=EBI-1951183, EBI-7813714;
CC P98161-3; Q13563-1: PKD2; NbExp=4; IntAct=EBI-15930070, EBI-9837017;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10339594,
CC ECO:0000269|PubMed:20980620, ECO:0000269|PubMed:27214281,
CC ECO:0000269|PubMed:27259053, ECO:0000269|PubMed:30093605}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:20980620,
CC ECO:0000269|PubMed:30093605}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:O08852}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O08852}. Golgi apparatus
CC {ECO:0000250|UniProtKB:O08852}. Note=PKD1 localization to the plasma
CC and ciliary membranes requires PKD2, is independent of PKD2 channel
CC activity, and involves stimulation of PKD1 autoproteolytic cleavage at
CC the GPS domain. PKD1:PKD2 interaction is required to reach the Golgi
CC apparatus from endoplasmic reticulum and then traffic to the cilia (By
CC similarity). Ciliary localization of PKD1 requires BBS1 and ARL6/BBS3
CC (By similarity). Cell surface localization requires GANAB
CC (PubMed:27259053). {ECO:0000250|UniProtKB:O08852,
CC ECO:0000269|PubMed:27259053}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P98161-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P98161-2; Sequence=VSP_009677, VSP_009678;
CC Name=3;
CC IsoId=P98161-3; Sequence=VSP_009678;
CC -!- DOMAIN: The LDL-receptor class A domain is atypical; the potential
CC calcium-binding site is missing.
CC -!- PTM: After synthesis, undergoes cleavage between Leu-3048 and Thr-3049
CC in the GPS domain. Cleavage at the GPS domain occurs through a cis-
CC autoproteolytic mechanism involving an ester-intermediate via N-O acyl
CC rearrangement. This process takes place in the early secretory pathway,
CC depends on initial N-glycosylation, and requires the REJ domain. There
CC is evidence that cleavage at GPS domain is incomplete. Uncleaved and
CC cleaved products may have different functions in vivo.
CC {ECO:0000269|PubMed:12482949}.
CC -!- DISEASE: Polycystic kidney disease 1 with or without polycystic liver
CC disease (PKD1) [MIM:173900]: An autosomal dominant disorder
CC characterized by renal cysts, liver cysts and intracranial aneurysm.
CC Clinical variability is due to differences in the rate of loss of
CC glomerular filtration, the age of reaching end-stage renal disease and
CC the occurrence of hypertension, symptomatic extrarenal cysts, and
CC subarachnoid hemorrhage from intracranial 'berry' aneurysm.
CC {ECO:0000269|PubMed:10200984, ECO:0000269|PubMed:10364515,
CC ECO:0000269|PubMed:10577909, ECO:0000269|PubMed:10647901,
CC ECO:0000269|PubMed:10729710, ECO:0000269|PubMed:10854095,
CC ECO:0000269|PubMed:10923040, ECO:0000269|PubMed:10987650,
CC ECO:0000269|PubMed:11012875, ECO:0000269|PubMed:11058904,
CC ECO:0000269|PubMed:11115377, ECO:0000269|PubMed:11216660,
CC ECO:0000269|PubMed:11316854, ECO:0000269|PubMed:11558899,
CC ECO:0000269|PubMed:11571556, ECO:0000269|PubMed:11691639,
CC ECO:0000269|PubMed:11773467, ECO:0000269|PubMed:11857740,
CC ECO:0000269|PubMed:11967008, ECO:0000269|PubMed:12007219,
CC ECO:0000269|PubMed:12070253, ECO:0000269|PubMed:12220456,
CC ECO:0000269|PubMed:12482949, ECO:0000269|PubMed:12842373,
CC ECO:0000269|PubMed:15772804, ECO:0000269|PubMed:18837007,
CC ECO:0000269|PubMed:21115670, ECO:0000269|PubMed:22508176,
CC ECO:0000269|PubMed:8554072, ECO:0000269|PubMed:9199561,
CC ECO:0000269|PubMed:9259200, ECO:0000269|PubMed:9285784,
CC ECO:0000269|PubMed:9521593, ECO:0000269|PubMed:9921908}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
CC -!- CAUTION: Variant Cys-2379 has been originally described as a benign
CC polymorphism (PubMed:10854095). However, it is a likely pathogenic
CC mutation (PubMed:22508176). {ECO:0000305|PubMed:10854095,
CC ECO:0000305|PubMed:22508176}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Polycystin-1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_204";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PKD1ID41725ch16p13.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U24497; AAC50128.1; -; mRNA.
DR EMBL; L33243; AAC37576.1; -; mRNA.
DR EMBL; L43619; AAC41765.1; -; Genomic_DNA.
DR EMBL; L43601; AAC41765.1; JOINED; Genomic_DNA.
DR EMBL; L43602; AAC41765.1; JOINED; Genomic_DNA.
DR EMBL; L43604; AAC41765.1; JOINED; Genomic_DNA.
DR EMBL; L43605; AAC41765.1; JOINED; Genomic_DNA.
DR EMBL; L43610; AAC41765.1; JOINED; Genomic_DNA.
DR EMBL; L43617; AAC41765.1; JOINED; Genomic_DNA.
DR EMBL; L43618; AAC41765.1; JOINED; Genomic_DNA.
DR EMBL; AC093513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS32369.1; -. [P98161-1]
DR CCDS; CCDS45385.1; -. [P98161-3]
DR PIR; A38971; A38971.
DR RefSeq; NP_000287.3; NM_000296.3. [P98161-3]
DR RefSeq; NP_001009944.2; NM_001009944.2. [P98161-1]
DR PDB; 1B4R; NMR; -; A=275-354.
DR PDB; 6A70; EM; 3.60 A; B=3049-4169.
DR PDBsum; 1B4R; -.
DR PDBsum; 6A70; -.
DR SMR; P98161; -.
DR BioGRID; 111327; 44.
DR ComplexPortal; CPX-4001; PKD1-PKD2 Polycystin complex.
DR CORUM; P98161; -.
DR DIP; DIP-52317N; -.
DR IntAct; P98161; 12.
DR MINT; P98161; -.
DR STRING; 9606.ENSP00000262304; -.
DR BindingDB; P98161; -.
DR ChEMBL; CHEMBL5772; -.
DR MEROPS; P02.036; -.
DR TCDB; 1.A.5.1.1; the polycystin cation channel (pcc) family.
DR GlyGen; P98161; 61 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P98161; -.
DR PhosphoSitePlus; P98161; -.
DR BioMuta; PKD1; -.
DR DMDM; 292495072; -.
DR EPD; P98161; -.
DR MassIVE; P98161; -.
DR MaxQB; P98161; -.
DR PaxDb; P98161; -.
DR PeptideAtlas; P98161; -.
DR PRIDE; P98161; -.
DR ProteomicsDB; 57797; -. [P98161-1]
DR ProteomicsDB; 57798; -. [P98161-2]
DR ProteomicsDB; 57799; -. [P98161-3]
DR Antibodypedia; 23502; 208 antibodies from 29 providers.
DR DNASU; 5310; -.
DR Ensembl; ENST00000262304.9; ENSP00000262304.4; ENSG00000008710.20. [P98161-1]
DR Ensembl; ENST00000423118.5; ENSP00000399501.1; ENSG00000008710.20. [P98161-3]
DR GeneID; 5310; -.
DR KEGG; hsa:5310; -.
DR MANE-Select; ENST00000262304.9; ENSP00000262304.4; NM_001009944.3; NP_001009944.3.
DR UCSC; uc002cos.1; human. [P98161-1]
DR CTD; 5310; -.
DR DisGeNET; 5310; -.
DR GeneCards; PKD1; -.
DR GeneReviews; PKD1; -.
DR HGNC; HGNC:9008; PKD1.
DR HPA; ENSG00000008710; Tissue enhanced (pituitary).
DR MalaCards; PKD1; -.
DR MIM; 173900; phenotype.
DR MIM; 601313; gene+phenotype.
DR neXtProt; NX_P98161; -.
DR OpenTargets; ENSG00000008710; -.
DR Orphanet; 730; Autosomal dominant polycystic kidney disease.
DR Orphanet; 88924; Autosomal dominant polycystic kidney disease type 1 with tuberous sclerosis.
DR PharmGKB; PA35521; -.
DR VEuPathDB; HostDB:ENSG00000008710; -.
DR eggNOG; KOG3599; Eukaryota.
DR GeneTree; ENSGT00940000158702; -.
DR HOGENOM; CLU_000173_0_0_1; -.
DR InParanoid; P98161; -.
DR OMA; LEAMMRI; -.
DR OrthoDB; 1276906at2759; -.
DR PhylomeDB; P98161; -.
DR TreeFam; TF316484; -.
DR PathwayCommons; P98161; -.
DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR SignaLink; P98161; -.
DR SIGNOR; P98161; -.
DR BioGRID-ORCS; 5310; 30 hits in 1084 CRISPR screens.
DR ChiTaRS; PKD1; human.
DR EvolutionaryTrace; P98161; -.
DR GeneWiki; PKD1; -.
DR GenomeRNAi; 5310; -.
DR Pharos; P98161; Tbio.
DR PRO; PR:P98161; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P98161; protein.
DR Bgee; ENSG00000008710; Expressed in right hemisphere of cerebellum and 201 other tissues.
DR ExpressionAtlas; P98161; baseline and differential.
DR Genevisible; P98161; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
DR GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
DR GO; GO:0034703; C:cation channel complex; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0060170; C:ciliary membrane; TAS:Reactome.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; NAS:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0031514; C:motile cilium; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0002133; C:polycystin complex; IPI:ComplexPortal.
DR GO; GO:0005262; F:calcium channel activity; ISS:BHF-UCL.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0042813; F:Wnt receptor activity; IDA:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:BHF-UCL.
DR GO; GO:0006816; P:calcium ion transport; IDA:ComplexPortal.
DR GO; GO:0007161; P:calcium-independent cell-matrix adhesion; TAS:ProtInc.
DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEP:UniProtKB.
DR GO; GO:0198738; P:cell-cell signaling by wnt; IDA:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; ISS:BHF-UCL.
DR GO; GO:0050982; P:detection of mechanical stimulus; ISS:BHF-UCL.
DR GO; GO:0048565; P:digestive tract development; IEP:UniProtKB.
DR GO; GO:0001892; P:embryonic placenta development; ISS:BHF-UCL.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:Ensembl.
DR GO; GO:0048806; P:genitalia development; IEP:UniProtKB.
DR GO; GO:0007507; P:heart development; IEP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; TAS:ProtInc.
DR GO; GO:0001701; P:in utero embryonic development; ISS:BHF-UCL.
DR GO; GO:0001822; P:kidney development; ISS:BHF-UCL.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0060428; P:lung epithelium development; IEP:UniProtKB.
DR GO; GO:0036303; P:lymph vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0072177; P:mesonephric duct development; IEP:UniProtKB.
DR GO; GO:0072164; P:mesonephric tubule development; IEP:UniProtKB.
DR GO; GO:0072218; P:metanephric ascending thin limb development; IEP:UniProtKB.
DR GO; GO:0072205; P:metanephric collecting duct development; IEP:UniProtKB.
DR GO; GO:0072287; P:metanephric distal tubule morphogenesis; IEP:UniProtKB.
DR GO; GO:0072237; P:metanephric proximal tubule development; IEP:UniProtKB.
DR GO; GO:0021915; P:neural tube development; IEP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:BHF-UCL.
DR GO; GO:0060674; P:placenta blood vessel development; ISS:BHF-UCL.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0006611; P:protein export from nucleus; ISS:BHF-UCL.
DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISS:BHF-UCL.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:BHF-UCL.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IDA:BHF-UCL.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IEA:Ensembl.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:MGI.
DR GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IEP:UniProtKB.
DR GO; GO:0021510; P:spinal cord development; IEP:UniProtKB.
DR CDD; cd01752; PLAT_polycystin; 1.
DR Gene3D; 2.60.40.10; -; 11.
DR Gene3D; 3.10.100.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR000434; PC1.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR002859; PKD/REJ-like.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR042060; PLAT_polycystin1.
DR InterPro; IPR006228; Polycystin_cat.
DR InterPro; IPR014010; REJ_dom.
DR InterPro; IPR002889; WSC_carb-bd.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00801; PKD; 15.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF02010; REJ; 1.
DR Pfam; PF01822; WSC; 1.
DR PRINTS; PR00500; POLYCYSTIN1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00308; LH2; 1.
DR SMART; SM00369; LRR_TYP; 2.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SMART; SM00089; PKD; 15.
DR SMART; SM00321; WSC; 1.
DR SUPFAM; SSF49299; SSF49299; 13.
DR SUPFAM; SSF49723; SSF49723; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR TIGRFAMs; TIGR00864; PCC; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS50093; PKD; 12.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS51111; REJ; 1.
DR PROSITE; PS51212; WSC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autocatalytic cleavage; Cell membrane;
KW Cell projection; Ciliopathy; Cilium; Coiled coil; Disease variant;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Lectin; Leucine-rich repeat; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..4303
FT /note="Polycystin-1"
FT /id="PRO_0000024298"
FT TOPO_DOM 24..3074
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TRANSMEM 3075..3095
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TOPO_DOM 3096..3277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TRANSMEM 3278..3298
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TOPO_DOM 3299..3323
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TRANSMEM 3324..3344
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TOPO_DOM 3345..3559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TRANSMEM 3560..3580
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TOPO_DOM 3581..3582
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TRANSMEM 3583..3603
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TOPO_DOM 3604..3665
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TRANSMEM 3666..3686
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TOPO_DOM 3687..3901
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TRANSMEM 3902..3922
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TOPO_DOM 3923..3935
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TRANSMEM 3936..3956
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TOPO_DOM 3957..3984
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TRANSMEM 3985..4005
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TOPO_DOM 4006..4027
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TRANSMEM 4028..4048
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TOPO_DOM 4049..4090
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TRANSMEM 4091..4110
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30093605"
FT TOPO_DOM 4111..4303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30093605"
FT DOMAIN 24..67
FT /note="LRRNT"
FT REPEAT 68..91
FT /note="LRR 1"
FT REPEAT 92..113
FT /note="LRR 2"
FT DOMAIN 125..178
FT /note="LRRCT"
FT DOMAIN 177..271
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT DOMAIN 272..359
FT /note="PKD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 415..531
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 638..671
FT /note="LDL-receptor class A; atypical"
FT DOMAIN 743..817
FT /note="PKD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 855..928
FT /note="PKD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 935..1020
FT /note="PKD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1023..1129
FT /note="PKD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1127..1215
FT /note="PKD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1213..1298
FT /note="PKD 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1294..1383
FT /note="PKD 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1382..1469
FT /note="PKD 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1468..1551
FT /note="PKD 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1550..1635
FT /note="PKD 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1634..1721
FT /note="PKD 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1719..1805
FT /note="PKD 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1807..1890
FT /note="PKD 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1889..1974
FT /note="PKD 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1977..2057
FT /note="PKD 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 2060..2148
FT /note="PKD 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 2146..2833
FT /note="REJ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00511"
FT DOMAIN 3012..3061
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT DOMAIN 3118..3233
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 616..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4160..4196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4243..4303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4220..4251
FT /evidence="ECO:0000255"
FT COMPBIAS 616..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4182..4196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4243..4258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 3048..3049
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:12482949,
FT ECO:0000269|PubMed:17525154"
FT MOD_RES 4166
FT /note="Phosphoserine; by PRKX; in vitro"
FT /evidence="ECO:0000269|PubMed:17980165"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 632
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 854
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 890
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1004
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1034
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1072
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1834
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1867
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2050
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2074
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 436..530
FT /evidence="ECO:0000250"
FT DISULFID 508..522
FT /evidence="ECO:0000250"
FT DISULFID 640..653
FT /evidence="ECO:0000250"
FT DISULFID 647..665
FT /evidence="ECO:0000250"
FT DISULFID 660..669
FT /evidence="ECO:0000250"
FT VAR_SEQ 2497..2507
FT /note="GWHDAEDAGAP -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7663510"
FT /id="VSP_009677"
FT VAR_SEQ 3390
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:7663510"
FT /id="VSP_009678"
FT VARIANT 13
FT /note="L -> Q (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011030"
FT VARIANT 36
FT /note="P -> H (in dbSNP:rs560049593)"
FT /evidence="ECO:0000269|PubMed:15772804,
FT ECO:0000269|PubMed:18837007"
FT /id="VAR_058759"
FT VARIANT 61
FT /note="P -> L (in PKD1; unknown pathological significance;
FT dbSNP:rs886038369)"
FT /evidence="ECO:0000269|PubMed:11967008,
FT ECO:0000269|PubMed:18837007"
FT /id="VAR_058760"
FT VARIANT 75
FT /note="S -> F (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011031"
FT VARIANT 87
FT /note="L -> M"
FT /evidence="ECO:0000269|PubMed:12007219"
FT /id="VAR_058761"
FT VARIANT 88
FT /note="A -> V (in dbSNP:rs958271752)"
FT /evidence="ECO:0000269|PubMed:11316854"
FT /id="VAR_012452"
FT VARIANT 97
FT /note="D -> G (in PKD1)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064380"
FT VARIANT 99
FT /note="S -> I (in PKD1; unknown pathological significance;
FT nearly abolishes expression at the cell membrane;
FT dbSNP:rs1567219544)"
FT /evidence="ECO:0000269|PubMed:18837007,
FT ECO:0000269|PubMed:27214281"
FT /id="VAR_058762"
FT VARIANT 139
FT /note="W -> C (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011032"
FT VARIANT 164
FT /note="Q -> R (in PKD1)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058763"
FT VARIANT 210
FT /note="C -> G (in PKD1)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058764"
FT VARIANT 324
FT /note="R -> L (in PKD1; dbSNP:rs199476099)"
FT /evidence="ECO:0000269|PubMed:10364515"
FT /id="VAR_010085"
FT VARIANT 325
FT /note="Y -> C (in PKD1; dbSNP:rs1232180956)"
FT /evidence="ECO:0000269|PubMed:22508176"
FT /id="VAR_068024"
FT VARIANT 381
FT /note="G -> C (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11857740"
FT /id="VAR_058765"
FT VARIANT 436
FT /note="C -> R (in PKD1; dbSNP:rs1555458892)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064381"
FT VARIANT 442
FT /note="A -> P (in PKD1)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064382"
FT VARIANT 508
FT /note="C -> R (in PKD1; dbSNP:rs58598099)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058766"
FT VARIANT 572
FT /note="P -> S (in dbSNP:rs149022148)"
FT /evidence="ECO:0000269|PubMed:11967008"
FT /id="VAR_058767"
FT VARIANT 594
FT /note="F -> Y (in PKD1)"
FT /evidence="ECO:0000269|PubMed:18837007"
FT /id="VAR_058768"
FT VARIANT 611
FT /note="R -> W (in PKD1; dbSNP:rs1555458413)"
FT /evidence="ECO:0000269|PubMed:22508176"
FT /id="VAR_068025"
FT VARIANT 690
FT /note="V -> D (in PKD1)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058769"
FT VARIANT 698
FT /note="Y -> D (in PKD1)"
FT /evidence="ECO:0000269|PubMed:22508176"
FT /id="VAR_068026"
FT VARIANT 727
FT /note="L -> P (in PKD1; dbSNP:rs1616940)"
FT /evidence="ECO:0000269|PubMed:21115670,
FT ECO:0000269|PubMed:22508176"
FT /id="VAR_064383"
FT VARIANT 727
FT /note="L -> R (in PKD1)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064384"
FT VARIANT 738
FT /note="P -> R"
FT /id="VAR_058770"
FT VARIANT 739
FT /note="R -> Q (in dbSNP:rs40433)"
FT /evidence="ECO:0000269|PubMed:11857740,
FT ECO:0000269|PubMed:18837007, ECO:0000269|PubMed:7663510"
FT /id="VAR_058771"
FT VARIANT 845
FT /note="L -> S (in PKD1; dbSNP:rs199476100)"
FT /evidence="ECO:0000269|PubMed:10364515,
FT ECO:0000269|PubMed:15772804"
FT /id="VAR_010086"
FT VARIANT 950
FT /note="L -> P (in dbSNP:rs2369063)"
FT /id="VAR_056696"
FT VARIANT 967
FT /note="W -> R (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11316854"
FT /id="VAR_012453"
FT VARIANT 987
FT /note="Q -> H (in PKD1; dbSNP:rs1266492292)"
FT /evidence="ECO:0000269|PubMed:12070253"
FT /id="VAR_058772"
FT VARIANT 1092
FT /note="M -> T (in dbSNP:rs2549677)"
FT /evidence="ECO:0000269|PubMed:11857740,
FT ECO:0000269|PubMed:11967008, ECO:0000269|PubMed:18837007,
FT ECO:0000269|PubMed:7736581"
FT /id="VAR_056697"
FT VARIANT 1114
FT /note="L -> R (in dbSNP:rs241573)"
FT /id="VAR_056698"
FT VARIANT 1166
FT /note="G -> S (in PKD1; dbSNP:rs573566419)"
FT /evidence="ECO:0000269|PubMed:11012875"
FT /id="VAR_011033"
FT VARIANT 1168
FT /note="P -> S (in dbSNP:rs146887330)"
FT /evidence="ECO:0000269|PubMed:11967008"
FT /id="VAR_058773"
FT VARIANT 1206
FT /note="V -> G (in PKD1)"
FT /evidence="ECO:0000269|PubMed:22508176"
FT /id="VAR_068027"
FT VARIANT 1240
FT /note="Missing (in PKD1)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058774"
FT VARIANT 1242
FT /note="T -> M (in PKD1; unknown pathological significance;
FT dbSNP:rs1033550407)"
FT /evidence="ECO:0000269|PubMed:18837007"
FT /id="VAR_058775"
FT VARIANT 1340
FT /note="R -> W (in PKD1; likely benign variant;
FT dbSNP:rs143690392)"
FT /evidence="ECO:0000269|PubMed:11967008"
FT /id="VAR_058776"
FT VARIANT 1399
FT /note="W -> R (in dbSNP:rs116092985)"
FT /evidence="ECO:0000269|PubMed:10364515,
FT ECO:0000269|PubMed:10577909, ECO:0000269|PubMed:11857740,
FT ECO:0000269|PubMed:11967008, ECO:0000269|PubMed:12070253,
FT ECO:0000269|PubMed:18837007"
FT /id="VAR_010087"
FT VARIANT 1516
FT /note="A -> T (in dbSNP:rs148164067)"
FT /evidence="ECO:0000269|PubMed:18837007"
FT /id="VAR_058777"
FT VARIANT 1557
FT /note="R -> P (in dbSNP:rs241572)"
FT /id="VAR_056699"
FT VARIANT 1649
FT /note="T -> M (in dbSNP:rs761106434)"
FT /evidence="ECO:0000269|PubMed:11857740"
FT /id="VAR_058778"
FT VARIANT 1667
FT /note="T -> P (in PKD1)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058779"
FT VARIANT 1684
FT /note="S -> L (in dbSNP:rs139520275)"
FT /evidence="ECO:0000269|PubMed:11967008"
FT /id="VAR_058780"
FT VARIANT 1734
FT /note="T -> K (in dbSNP:rs241571)"
FT /id="VAR_056700"
FT VARIANT 1786
FT /note="P -> L (in dbSNP:rs151176070)"
FT /evidence="ECO:0000269|PubMed:10364515"
FT /id="VAR_010088"
FT VARIANT 1811
FT /note="E -> K (in PKD1; dbSNP:rs778028644)"
FT /evidence="ECO:0000269|PubMed:11967008,
FT ECO:0000269|PubMed:12842373"
FT /id="VAR_058781"
FT VARIANT 1871
FT /note="A -> T (in dbSNP:rs144137200)"
FT /evidence="ECO:0000269|PubMed:18837007"
FT /id="VAR_058782"
FT VARIANT 1926
FT /note="A -> V (in dbSNP:rs754890213)"
FT /evidence="ECO:0000269|PubMed:18837007"
FT /id="VAR_058783"
FT VARIANT 1943
FT /note="V -> I (in dbSNP:rs137978188)"
FT /evidence="ECO:0000269|PubMed:11967008"
FT /id="VAR_058784"
FT VARIANT 1952
FT /note="G -> D"
FT /evidence="ECO:0000269|PubMed:18837007"
FT /id="VAR_058785"
FT VARIANT 1956
FT /note="V -> E (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11012875"
FT /id="VAR_011034"
FT VARIANT 1992..1993
FT /note="FT -> L (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011035"
FT VARIANT 1995
FT /note="R -> H (in dbSNP:rs752388015)"
FT /evidence="ECO:0000269|PubMed:11012875"
FT /id="VAR_011036"
FT VARIANT 2083
FT /note="T -> I (in PKD1; dbSNP:rs1383930225)"
FT /evidence="ECO:0000269|PubMed:12007219"
FT /id="VAR_058786"
FT VARIANT 2092
FT /note="Y -> C (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11967008,
FT ECO:0000269|PubMed:12842373"
FT /id="VAR_058787"
FT VARIANT 2185
FT /note="Y -> D (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11857740"
FT /id="VAR_058788"
FT VARIANT 2200
FT /note="R -> C (in PKD1; likely benign variant;
FT dbSNP:rs140869992)"
FT /evidence="ECO:0000269|PubMed:12842373,
FT ECO:0000269|PubMed:18837007"
FT /id="VAR_058789"
FT VARIANT 2220..2224
FT /note="Missing (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011037"
FT VARIANT 2250
FT /note="T -> M (in PKD1; unknown pathological significance;
FT dbSNP:rs139971481)"
FT /evidence="ECO:0000269|PubMed:10854095"
FT /id="VAR_011038"
FT VARIANT 2260
FT /note="Missing (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11967008,
FT ECO:0000269|PubMed:12842373"
FT /id="VAR_058790"
FT VARIANT 2329
FT /note="R -> W (in PKD1; unknown pathological significance;
FT dbSNP:rs200433577)"
FT /evidence="ECO:0000269|PubMed:10854095"
FT /id="VAR_011039"
FT VARIANT 2336
FT /note="Y -> D (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011040"
FT VARIANT 2370
FT /note="C -> R (in PKD1; dbSNP:rs1567187445)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058791"
FT VARIANT 2373
FT /note="C -> Y (in PKD1)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058792"
FT VARIANT 2379
FT /note="Y -> C (in PKD1)"
FT /evidence="ECO:0000269|PubMed:10854095,
FT ECO:0000269|PubMed:22508176"
FT /id="VAR_011041"
FT VARIANT 2391
FT /note="G -> D (in PKD1)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064385"
FT VARIANT 2392
FT /note="R -> P (in PKD1)"
FT /evidence="ECO:0000269|PubMed:10577909"
FT /id="VAR_012454"
FT VARIANT 2408
FT /note="R -> C (in PKD1; dbSNP:rs538769374)"
FT /evidence="ECO:0000269|PubMed:11012875"
FT /id="VAR_011042"
FT VARIANT 2421
FT /note="Missing (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11857740"
FT /id="VAR_058793"
FT VARIANT 2422
FT /note="T -> K (in PKD1; dbSNP:rs1555453210)"
FT /evidence="ECO:0000269|PubMed:18837007"
FT /id="VAR_058794"
FT VARIANT 2423
FT /note="S -> F (in PKD1; dbSNP:rs1555453207)"
FT /evidence="ECO:0000269|PubMed:10577909"
FT /id="VAR_012455"
FT VARIANT 2434
FT /note="R -> W (in PKD1; dbSNP:rs151257298)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064386"
FT VARIANT 2443
FT /note="G -> GG (in PKD1)"
FT /id="VAR_011043"
FT VARIANT 2471
FT /note="P -> L (in PKD1; dbSNP:rs1161298621)"
FT /evidence="ECO:0000269|PubMed:11571556"
FT /id="VAR_012456"
FT VARIANT 2515
FT /note="R -> Q (in dbSNP:rs2432404)"
FT /id="VAR_056701"
FT VARIANT 2519
FT /note="Q -> L (in PKD1; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:11571556"
FT /id="VAR_012457"
FT VARIANT 2534
FT /note="S -> G (in dbSNP:rs3874655)"
FT /id="VAR_056702"
FT VARIANT 2546
FT /note="H -> Y (in PKD1; dbSNP:rs200037070)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064387"
FT VARIANT 2548
FT /note="E -> Q (in dbSNP:rs28369051)"
FT /evidence="ECO:0000269|PubMed:10577909"
FT /id="VAR_012458"
FT VARIANT 2569
FT /note="S -> C (in PKD1; dbSNP:rs758896945)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064388"
FT VARIANT 2579
FT /note="Missing (in PKD1; unknown pathological significance;
FT dbSNP:rs748240352)"
FT /evidence="ECO:0000269|PubMed:11571556"
FT /id="VAR_012459"
FT VARIANT 2582
FT /note="T -> M (in dbSNP:rs2432405)"
FT /evidence="ECO:0000269|PubMed:11571556"
FT /id="VAR_012460"
FT VARIANT 2604
FT /note="D -> N (in dbSNP:rs778565182)"
FT /evidence="ECO:0000269|PubMed:11012875"
FT /id="VAR_011044"
FT VARIANT 2613
FT /note="Missing (in PKD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:11571556"
FT /id="VAR_012461"
FT VARIANT 2638
FT /note="H -> R (in PKD1; benign variant; dbSNP:rs9936785)"
FT /evidence="ECO:0000269|PubMed:10577909,
FT ECO:0000269|PubMed:11571556, ECO:0000269|PubMed:11857740,
FT ECO:0000269|PubMed:11967008, ECO:0000269|PubMed:15772804,
FT ECO:0000269|PubMed:18837007"
FT /id="VAR_012462"
FT VARIANT 2646
FT /note="I -> T (in PKD1; dbSNP:rs374500158)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064389"
FT VARIANT 2649
FT /note="T -> I (in PKD1; unknown pathological significance;
FT dbSNP:rs1490043027)"
FT /evidence="ECO:0000269|PubMed:11571556"
FT /id="VAR_012463"
FT VARIANT 2674
FT /note="P -> S (in dbSNP:rs144557371)"
FT /evidence="ECO:0000269|PubMed:11115377,
FT ECO:0000269|PubMed:11967008"
FT /id="VAR_011045"
FT VARIANT 2696
FT /note="L -> R (in PKD1; dbSNP:rs201238819)"
FT /evidence="ECO:0000269|PubMed:11316854"
FT /id="VAR_012464"
FT VARIANT 2708
FT /note="T -> M (in dbSNP:rs147350387)"
FT /evidence="ECO:0000269|PubMed:11115377,
FT ECO:0000269|PubMed:11967008, ECO:0000269|PubMed:18837007"
FT /id="VAR_011046"
FT VARIANT 2734
FT /note="P -> T (in dbSNP:rs150568356)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011047"
FT VARIANT 2735
FT /note="Q -> L (in dbSNP:rs141717814)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011048"
FT VARIANT 2746
FT /note="R -> P (in dbSNP:rs1800569)"
FT /id="VAR_014918"
FT VARIANT 2752
FT /note="A -> D (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011049"
FT VARIANT 2760
FT /note="M -> T (associated with PKD1; dbSNP:rs1800568)"
FT /evidence="ECO:0000269|PubMed:9285784"
FT /id="VAR_005533"
FT VARIANT 2761
FT /note="R -> P (associated with PKD1)"
FT /evidence="ECO:0000269|PubMed:9285784"
FT /id="VAR_058795"
FT VARIANT 2763
FT /note="L -> V (in PKD1)"
FT /evidence="ECO:0000269|PubMed:9285784"
FT /id="VAR_005535"
FT VARIANT 2764
FT /note="M -> T (associated with PKD1; dbSNP:rs1596527405)"
FT /evidence="ECO:0000269|PubMed:9285784"
FT /id="VAR_005536"
FT VARIANT 2765
FT /note="R -> C (in dbSNP:rs144979397)"
FT /evidence="ECO:0000269|PubMed:11115377,
FT ECO:0000269|PubMed:11857740"
FT /id="VAR_011051"
FT VARIANT 2765
FT /note="R -> RILMR (in PKD1)"
FT /id="VAR_011050"
FT VARIANT 2767
FT /note="R -> C (in PKD1)"
FT /evidence="ECO:0000269|PubMed:22508176"
FT /id="VAR_068028"
FT VARIANT 2768
FT /note="V -> M (in PKD1; associated with S-2858;
FT dbSNP:rs1456510041)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011052"
FT VARIANT 2771
FT /note="E -> K (in PKD1; does not undergo autoproteolytic
FT cleavage; dbSNP:rs1057518897)"
FT /evidence="ECO:0000269|PubMed:11115377,
FT ECO:0000269|PubMed:12482949, ECO:0000269|PubMed:12842373,
FT ECO:0000269|PubMed:22508176"
FT /id="VAR_011053"
FT VARIANT 2782
FT /note="V -> M (in dbSNP:rs151089809)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011054"
FT VARIANT 2785
FT /note="G -> D (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11857740"
FT /id="VAR_058796"
FT VARIANT 2791
FT /note="R -> Q (in a patient with polycystic kidney disease;
FT does not affect autoproteolytic cleavage at the GPS domain;
FT dbSNP:rs367746233)"
FT /evidence="ECO:0000269|PubMed:12482949,
FT ECO:0000269|PubMed:9285784"
FT /id="VAR_005537"
FT VARIANT 2802
FT /note="P -> L (in PKD1; dbSNP:rs534112936)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058797"
FT VARIANT 2814
FT /note="G -> R (in PKD1; likely benign variant;
FT dbSNP:rs149151043)"
FT /evidence="ECO:0000269|PubMed:11115377,
FT ECO:0000269|PubMed:11967008, ECO:0000269|PubMed:12007219,
FT ECO:0000269|PubMed:18837007"
FT /id="VAR_011055"
FT VARIANT 2816
FT /note="L -> P (in PKD1; dbSNP:rs1567177684)"
FT /evidence="ECO:0000269|PubMed:11115377,
FT ECO:0000269|PubMed:12007219"
FT /id="VAR_011056"
FT VARIANT 2826
FT /note="I -> T (in PKD1)"
FT /evidence="ECO:0000269|PubMed:9285784"
FT /id="VAR_005538"
FT VARIANT 2858
FT /note="G -> S (in PKD1; associated with M-2768;
FT dbSNP:rs755522953)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011057"
FT VARIANT 2888
FT /note="R -> G"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011058"
FT VARIANT 2889
FT /note="S -> R (in PKD1; dbSNP:rs752447240)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064390"
FT VARIANT 2905
FT /note="V -> I (in dbSNP:rs147788838)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011059"
FT VARIANT 2921
FT /note="H -> P (in PKD1; does not undergo autoproteolytic
FT cleavage)"
FT /evidence="ECO:0000269|PubMed:10923040,
FT ECO:0000269|PubMed:12482949"
FT /id="VAR_011060"
FT VARIANT 2958
FT /note="S -> L (in dbSNP:rs750780241)"
FT /evidence="ECO:0000269|PubMed:11967008"
FT /id="VAR_058798"
FT VARIANT 2966
FT /note="E -> D (in dbSNP:rs13337123)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011061"
FT VARIANT 2972
FT /note="D -> N (in dbSNP:rs150189496)"
FT /evidence="ECO:0000269|PubMed:11571556"
FT /id="VAR_012465"
FT VARIANT 2977
FT /note="T -> N"
FT /evidence="ECO:0000269|PubMed:11967008"
FT /id="VAR_058799"
FT VARIANT 2978
FT /note="Missing (in PKD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:11571556"
FT /id="VAR_012466"
FT VARIANT 2985
FT /note="R -> G (in PKD1; dbSNP:rs373952574)"
FT /evidence="ECO:0000269|PubMed:11316854"
FT /id="VAR_012467"
FT VARIANT 2993
FT /note="L -> P (in PKD1; does not undergo autoproteolytic
FT cleavage; dbSNP:rs1555450487)"
FT /evidence="ECO:0000269|PubMed:12482949,
FT ECO:0000269|PubMed:9199561"
FT /id="VAR_010089"
FT VARIANT 2995
FT /note="L -> R (in PKD1)"
FT /evidence="ECO:0000269|PubMed:22508176"
FT /id="VAR_068029"
FT VARIANT 3005
FT /note="Q -> E (in dbSNP:rs1063401)"
FT /id="VAR_056703"
FT VARIANT 3008
FT /note="V -> L (in PKD1)"
FT /evidence="ECO:0000269|PubMed:9285784"
FT /id="VAR_005539"
FT VARIANT 3008
FT /note="V -> M (in dbSNP:rs117896488)"
FT /evidence="ECO:0000269|PubMed:11558899"
FT /id="VAR_058800"
FT VARIANT 3012..3017
FT /note="Missing (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11115377"
FT /id="VAR_011062"
FT VARIANT 3016
FT /note="Q -> R (in PKD1; does not undergo autoproteolytic
FT cleavage)"
FT /evidence="ECO:0000269|PubMed:12482949,
FT ECO:0000269|PubMed:9199561"
FT /id="VAR_010090"
FT VARIANT 3023
FT /note="M -> V (in dbSNP:rs17135779)"
FT /id="VAR_056704"
FT VARIANT 3027..3039
FT /note="Missing (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11857740"
FT /id="VAR_058801"
FT VARIANT 3039
FT /note="R -> C (in PKD1; dbSNP:rs200522524)"
FT /evidence="ECO:0000269|PubMed:11316854"
FT /id="VAR_012468"
FT VARIANT 3057
FT /note="V -> M (in dbSNP:rs778055216)"
FT /evidence="ECO:0000269|PubMed:11967008"
FT /id="VAR_058802"
FT VARIANT 3066
FT /note="F -> L (in PKD1; dbSNP:rs9925969)"
FT /evidence="ECO:0000269|PubMed:10854095,
FT ECO:0000269|PubMed:10923040, ECO:0000269|PubMed:11115377,
FT ECO:0000269|PubMed:11571556, ECO:0000269|PubMed:11857740,
FT ECO:0000269|PubMed:15772804, ECO:0000269|PubMed:18837007,
FT ECO:0000269|PubMed:9285784"
FT /id="VAR_011063"
FT VARIANT 3138
FT /note="V -> M (in PKD1; unknown pathological significance;
FT dbSNP:rs1358566538)"
FT /evidence="ECO:0000269|PubMed:15772804"
FT /id="VAR_058803"
FT VARIANT 3139
FT /note="G -> V"
FT /evidence="ECO:0000269|PubMed:10854095"
FT /id="VAR_011064"
FT VARIANT 3154
FT /note="L -> P (in PKD1)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064391"
FT VARIANT 3167
FT /note="I -> F (in PKD1; dbSNP:rs139945204)"
FT /evidence="ECO:0000269|PubMed:11967008"
FT /id="VAR_058804"
FT VARIANT 3188
FT /note="Missing (in PKD1)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058805"
FT VARIANT 3193
FT /note="P -> L"
FT /evidence="ECO:0000269|PubMed:10854095"
FT /id="VAR_011065"
FT VARIANT 3247
FT /note="R -> H (in PKD1; dbSNP:rs140791671)"
FT /evidence="ECO:0000269|PubMed:11216660"
FT /id="VAR_013838"
FT VARIANT 3285
FT /note="V -> I (in PKD1; dbSNP:rs201780393)"
FT /evidence="ECO:0000269|PubMed:11316854"
FT /id="VAR_012469"
FT VARIANT 3311
FT /note="H -> R (in dbSNP:rs1242837732)"
FT /evidence="ECO:0000269|PubMed:11316854"
FT /id="VAR_012470"
FT VARIANT 3355
FT /note="P -> L (in PKD1; dbSNP:rs781263445)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058806"
FT VARIANT 3375
FT /note="V -> M (in PKD1; dbSNP:rs371283948)"
FT /evidence="ECO:0000269|PubMed:10923040,
FT ECO:0000269|PubMed:9921908"
FT /id="VAR_005541"
FT VARIANT 3382
FT /note="T -> M (in PKD1; dbSNP:rs776463508)"
FT /evidence="ECO:0000269|PubMed:11216660"
FT /id="VAR_013839"
FT VARIANT 3435
FT /note="R -> Q (in dbSNP:rs140189010)"
FT /evidence="ECO:0000269|PubMed:11967008"
FT /id="VAR_058807"
FT VARIANT 3510
FT /note="T -> M (in dbSNP:rs45478794)"
FT /evidence="ECO:0000269|PubMed:11558899,
FT ECO:0000269|PubMed:11691639, ECO:0000269|PubMed:12007219,
FT ECO:0000269|PubMed:15772804, ECO:0000269|PubMed:9199561"
FT /id="VAR_010091"
FT VARIANT 3511
FT /note="L -> V (in PKD1; unknown pathological significance;
FT dbSNP:rs141946034)"
FT /evidence="ECO:0000269|PubMed:9199561"
FT /id="VAR_010092"
FT VARIANT 3512
FT /note="A -> V (in dbSNP:rs34197769)"
FT /evidence="ECO:0000269|PubMed:11967008,
FT ECO:0000269|PubMed:15772804, ECO:0000269|PubMed:18837007"
FT /id="VAR_011066"
FT VARIANT 3560
FT /note="G -> R (in PKD1; dbSNP:rs79000340)"
FT /evidence="ECO:0000269|PubMed:11691639"
FT /id="VAR_012471"
FT VARIANT 3562
FT /note="S -> N"
FT /id="VAR_010093"
FT VARIANT 3602
FT /note="G -> S (in PKD1; dbSNP:rs781492044)"
FT /evidence="ECO:0000269|PubMed:12220456"
FT /id="VAR_058808"
FT VARIANT 3603
FT /note="W -> R (in PKD1)"
FT /evidence="ECO:0000269|PubMed:21115670"
FT /id="VAR_064392"
FT VARIANT 3632
FT /note="E -> D (in PKD1; dbSNP:rs1416373452)"
FT /evidence="ECO:0000269|PubMed:11773467,
FT ECO:0000269|PubMed:8554072"
FT /id="VAR_005542"
FT VARIANT 3649
FT /note="P -> L (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11773467"
FT /id="VAR_058809"
FT VARIANT 3651
FT /note="G -> S (in PKD1)"
FT /evidence="ECO:0000269|PubMed:22508176"
FT /id="VAR_068030"
FT VARIANT 3678
FT /note="M -> T (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11773467,
FT ECO:0000269|PubMed:9259200"
FT /id="VAR_005543"
FT VARIANT 3682
FT /note="L -> P (in PKD1)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058810"
FT VARIANT 3719
FT /note="R -> Q (in PKD1; dbSNP:rs1555446576)"
FT /evidence="ECO:0000269|PubMed:11058904,
FT ECO:0000269|PubMed:11691639"
FT /id="VAR_011067"
FT VARIANT 3726
FT /note="W -> S (in PKD1; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:18837007"
FT /id="VAR_058811"
FT VARIANT 3748..3752
FT /note="Missing (in PKD1)"
FT /evidence="ECO:0000269|PubMed:10647901,
FT ECO:0000269|PubMed:8554072"
FT /id="VAR_005544"
FT VARIANT 3750
FT /note="R -> Q (in PKD1; dbSNP:rs1327414405)"
FT /evidence="ECO:0000269|PubMed:21115670,
FT ECO:0000269|PubMed:22508176"
FT /id="VAR_064393"
FT VARIANT 3751
FT /note="Q -> R (in PKD1)"
FT /evidence="ECO:0000269|PubMed:12842373"
FT /id="VAR_058812"
FT VARIANT 3753
FT /note="R -> W (in PKD1; dbSNP:rs1167476946)"
FT /evidence="ECO:0000269|PubMed:10729710,
FT ECO:0000269|PubMed:11691639, ECO:0000269|PubMed:22508176"
FT /id="VAR_011068"
FT VARIANT 3815
FT /note="D -> N (in PKD1)"
FT /evidence="ECO:0000269|PubMed:10729710"
FT /id="VAR_011069"
FT VARIANT 3852
FT /note="L -> P (in PKD1)"
FT /evidence="ECO:0000269|PubMed:11058904,
FT ECO:0000269|PubMed:11967008"
FT /id="VAR_011070"
FT VARIANT 3954
FT /note="A -> P (in PKD1; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:15772804"
FT /id="VAR_058813"
FT VARIANT 3996
FT /note="F -> FLLF (in PKD1)"
FT /id="VAR_010094"
FT VARIANT 4032
FT /note="G -> D (in PKD1; dbSNP:rs142768096)"
FT /evidence="ECO:0000269|PubMed:9521593"
FT /id="VAR_005545"
FT VARIANT 4045
FT /note="I -> V (in dbSNP:rs10960)"
FT /evidence="ECO:0000269|PubMed:10647901,
FT ECO:0000269|PubMed:11058904, ECO:0000269|PubMed:11773467,
FT ECO:0000269|PubMed:11967008, ECO:0000269|PubMed:12070253,
FT ECO:0000269|PubMed:15772804, ECO:0000269|PubMed:18837007,
FT ECO:0000269|PubMed:9521593"
FT /id="VAR_005546"
FT VARIANT 4058
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:9150733"
FT /id="VAR_005547"
FT VARIANT 4059
FT /note="A -> V (in dbSNP:rs3209986)"
FT /evidence="ECO:0000269|PubMed:11773467,
FT ECO:0000269|PubMed:11967008, ECO:0000269|PubMed:15772804,
FT ECO:0000269|PubMed:18837007"
FT /id="VAR_010095"
FT VARIANT 4102
FT /note="G -> E (in dbSNP:rs1306483854)"
FT /evidence="ECO:0000269|PubMed:11773467"
FT /id="VAR_058814"
FT VARIANT 4106
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:11773467"
FT /id="VAR_058815"
FT VARIANT 4124
FT /note="P -> S (in dbSNP:rs1309138642)"
FT /evidence="ECO:0000269|PubMed:11967008"
FT /id="VAR_058816"
FT VARIANT 4132
FT /note="Missing (in PKD1)"
FT /evidence="ECO:0000269|PubMed:10647901"
FT /id="VAR_011071"
FT VARIANT 4136
FT /note="R -> G (in PKD1)"
FT /evidence="ECO:0000269|PubMed:10987650"
FT /id="VAR_010096"
FT VARIANT 4146
FT /note="V -> I (in dbSNP:rs148478410)"
FT /evidence="ECO:0000269|PubMed:11773467,
FT ECO:0000269|PubMed:11967008"
FT /id="VAR_058817"
FT VARIANT 4150
FT /note="R -> C (in PKD1; dbSNP:rs1282668884)"
FT /evidence="ECO:0000269|PubMed:22508176"
FT /id="VAR_068031"
FT VARIANT 4154
FT /note="R -> C (in PKD1; dbSNP:rs115538130)"
FT /evidence="ECO:0000269|PubMed:10987650"
FT /id="VAR_010097"
FT VARIANT 4155
FT /note="F -> V (in PKD1)"
FT /evidence="ECO:0000269|PubMed:18837007"
FT /id="VAR_058818"
FT VARIANT 4190
FT /note="S -> F (in dbSNP:rs547854563)"
FT /evidence="ECO:0000269|PubMed:11967008,
FT ECO:0000269|PubMed:9199561"
FT /id="VAR_010098"
FT VARIANT 4225
FT /note="Q -> P (in PKD1)"
FT /evidence="ECO:0000269|PubMed:10200984"
FT /id="VAR_010099"
FT VARIANT 4255
FT /note="P -> S (in PKD1)"
FT /evidence="ECO:0000269|PubMed:12220456"
FT /id="VAR_058819"
FT VARIANT 4276
FT /note="R -> W (in PKD1; dbSNP:rs114251396)"
FT /evidence="ECO:0000269|PubMed:10200984,
FT ECO:0000269|PubMed:22508176"
FT /id="VAR_010100"
FT MUTAGEN 3049
FT /note="T->C,S: Does not affect auto-cleavage."
FT /evidence="ECO:0000269|PubMed:17525154"
FT MUTAGEN 3049
FT /note="T->G,R,V: Does not undergo auto-cleavage."
FT /evidence="ECO:0000269|PubMed:17525154"
FT CONFLICT 71
FT /note="A -> E (in Ref. 1; AAC50128)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="R -> Q (in Ref. 1; AAC50128)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="P -> A (in Ref. 1; AAC50128)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="A -> D (in Ref. 1; AAC50128)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="P -> A (in Ref. 2; AAC37576/AAC41765)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="A -> G (in Ref. 1; AAC50128)"
FT /evidence="ECO:0000305"
FT CONFLICT 774..775
FT /note="AT -> QR (in Ref. 1; AAC50128)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="L -> M (in Ref. 2; AAC37576/AAC41765)"
FT /evidence="ECO:0000305"
FT CONFLICT 866
FT /note="V -> L (in Ref. 1; AAC50128)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="G -> A (in Ref. 1; AAC50128)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056
FT /note="T -> N (in Ref. 2; AAC37576/AAC41765)"
FT /evidence="ECO:0000305"
FT CONFLICT 1277
FT /note="A -> G (in Ref. 1; AAC50128)"
FT /evidence="ECO:0000305"
FT CONFLICT 1724
FT /note="A -> T (in Ref. 2; AAC37576/AAC41765)"
FT /evidence="ECO:0000305"
FT CONFLICT 1976
FT /note="V -> M (in Ref. 2; AAC37576/AAC41765)"
FT /evidence="ECO:0000305"
FT CONFLICT 3982..3983
FT /note="QL -> HV (in Ref. 1; AAC50128)"
FT /evidence="ECO:0000305"
FT CONFLICT 4005..4006
FT /note="QL -> HV (in Ref. 1; AAC50128)"
FT /evidence="ECO:0000305"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1B4R"
FT STRAND 285..296
FT /evidence="ECO:0007829|PDB:1B4R"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:1B4R"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:1B4R"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:1B4R"
FT STRAND 327..338
FT /evidence="ECO:0007829|PDB:1B4R"
FT STRAND 343..353
FT /evidence="ECO:0007829|PDB:1B4R"
SQ SEQUENCE 4303 AA; 462529 MW; AEDAC48F3F0A853C CRC64;
MPPAAPARLA LALGLGLWLG ALAGGPGRGC GPCEPPCLCG PAPGAACRVN CSGRGLRTLG
PALRIPADAT ALDVSHNLLR ALDVGLLANL SALAELDISN NKISTLEEGI FANLFNLSEI
NLSGNPFECD CGLAWLPRWA EEQQVRVVQP EAATCAGPGS LAGQPLLGIP LLDSGCGEEY
VACLPDNSSG TVAAVSFSAA HEGLLQPEAC SAFCFSTGQG LAALSEQGWC LCGAAQPSSA
SFACLSLCSG PPPPPAPTCR GPTLLQHVFP ASPGATLVGP HGPLASGQLA AFHIAAPLPV
TATRWDFGDG SAEVDAAGPA ASHRYVLPGR YHVTAVLALG AGSALLGTDV QVEAAPAALE
LVCPSSVQSD ESLDLSIQNR GGSGLEAAYS IVALGEEPAR AVHPLCPSDT EIFPGNGHCY
RLVVEKAAWL QAQEQCQAWA GAALAMVDSP AVQRFLVSRV TRSLDVWIGF STVQGVEVGP
APQGEAFSLE SCQNWLPGEP HPATAEHCVR LGPTGWCNTD LCSAPHSYVC ELQPGGPVQD
AENLLVGAPS GDLQGPLTPL AQQDGLSAPH EPVEVMVFPG LRLSREAFLT TAEFGTQELR
RPAQLRLQVY RLLSTAGTPE NGSEPESRSP DNRTQLAPAC MPGGRWCPGA NICLPLDASC
HPQACANGCT SGPGLPGAPY ALWREFLFSV PAGPPAQYSV TLHGQDVLML PGDLVGLQHD
AGPGALLHCS PAPGHPGPRA PYLSANASSW LPHLPAQLEG TWACPACALR LLAATEQLTV
LLGLRPNPGL RLPGRYEVRA EVGNGVSRHN LSCSFDVVSP VAGLRVIYPA PRDGRLYVPT
NGSALVLQVD SGANATATAR WPGGSVSARF ENVCPALVAT FVPGCPWETN DTLFSVVALP
WLSEGEHVVD VVVENSASRA NLSLRVTAEE PICGLRATPS PEARVLQGVL VRYSPVVEAG
SDMVFRWTIN DKQSLTFQNV VFNVIYQSAA VFKLSLTASN HVSNVTVNYN VTVERMNRMQ
GLQVSTVPAV LSPNATLALT AGVLVDSAVE VAFLWTFGDG EQALHQFQPP YNESFPVPDP
SVAQVLVEHN VMHTYAAPGE YLLTVLASNA FENLTQQVPV SVRASLPSVA VGVSDGVLVA
GRPVTFYPHP LPSPGGVLYT WDFGDGSPVL TQSQPAANHT YASRGTYHVR LEVNNTVSGA
AAQADVRVFE ELRGLSVDMS LAVEQGAPVV VSAAVQTGDN ITWTFDMGDG TVLSGPEATV
EHVYLRAQNC TVTVGAASPA GHLARSLHVL VFVLEVLRVE PAACIPTQPD ARLTAYVTGN
PAHYLFDWTF GDGSSNTTVR GCPTVTHNFT RSGTFPLALV LSSRVNRAHY FTSICVEPEV
GNVTLQPERQ FVQLGDEAWL VACAWPPFPY RYTWDFGTEE AAPTRARGPE VTFIYRDPGS
YLVTVTASNN ISAANDSALV EVQEPVLVTS IKVNGSLGLE LQQPYLFSAV GRGRPASYLW
DLGDGGWLEG PEVTHAYNST GDFTVRVAGW NEVSRSEAWL NVTVKRRVRG LVVNASRTVV
PLNGSVSFST SLEAGSDVRY SWVLCDRCTP IPGGPTISYT FRSVGTFNII VTAENEVGSA
QDSIFVYVLQ LIEGLQVVGG GRYFPTNHTV QLQAVVRDGT NVSYSWTAWR DRGPALAGSG
KGFSLTVLEA GTYHVQLRAT NMLGSAWADC TMDFVEPVGW LMVAASPNPA AVNTSVTLSA
ELAGGSGVVY TWSLEEGLSW ETSEPFTTHS FPTPGLHLVT MTAGNPLGSA NATVEVDVQV
PVSGLSIRAS EPGGSFVAAG SSVPFWGQLA TGTNVSWCWA VPGGSSKRGP HVTMVFPDAG
TFSIRLNASN AVSWVSATYN LTAEEPIVGL VLWASSKVVA PGQLVHFQIL LAAGSAVTFR
LQVGGANPEV LPGPRFSHSF PRVGDHVVSV RGKNHVSWAQ AQVRIVVLEA VSGLQVPNCC
EPGIATGTER NFTARVQRGS RVAYAWYFSL QKVQGDSLVI LSGRDVTYTP VAAGLLEIQV
RAFNALGSEN RTLVLEVQDA VQYVALQSGP CFTNRSAQFE AATSPSPRRV AYHWDFGDGS
PGQDTDEPRA EHSYLRPGDY RVQVNASNLV SFFVAQATVT VQVLACREPE VDVVLPLQVL
MRRSQRNYLE AHVDLRDCVT YQTEYRWEVY RTASCQRPGR PARVALPGVD VSRPRLVLPR
LALPVGHYCF VFVVSFGDTP LTQSIQANVT VAPERLVPII EGGSYRVWSD TRDLVLDGSE
SYDPNLEDGD QTPLSFHWAC VASTQREAGG CALNFGPRGS STVTIPRERL AAGVEYTFSL
TVWKAGRKEE ATNQTVLIRS GRVPIVSLEC VSCKAQAVYE VSRSSYVYLE GRCLNCSSGS
KRGRWAARTF SNKTLVLDET TTSTGSAGMR LVLRRGVLRD GEGYTFTLTV LGRSGEEEGC
ASIRLSPNRP PLGGSCRLFP LGAVHALTTK VHFECTGWHD AEDAGAPLVY ALLLRRCRQG
HCEEFCVYKG SLSSYGAVLP PGFRPHFEVG LAVVVQDQLG AAVVALNRSL AITLPEPNGS
ATGLTVWLHG LTASVLPGLL RQADPQHVIE YSLALVTVLN EYERALDVAA EPKHERQHRA
QIRKNITETL VSLRVHTVDD IQQIAAALAQ CMGPSRELVC RSCLKQTLHK LEAMMLILQA
ETTAGTVTPT AIGDSILNIT GDLIHLASSD VRAPQPSELG AESPSRMVAS QAYNLTSALM
RILMRSRVLN EEPLTLAGEE IVAQGKRSDP RSLLCYGGAP GPGCHFSIPE AFSGALANLS
DVVQLIFLVD SNPFPFGYIS NYTVSTKVAS MAFQTQAGAQ IPIERLASER AITVKVPNNS
DWAARGHRSS ANSANSVVVQ PQASVGAVVT LDSSNPAAGL HLQLNYTLLD GHYLSEEPEP
YLAVYLHSEP RPNEHNCSAS RRIRPESLQG ADHRPYTFFI SPGSRDPAGS YHLNLSSHFR
WSALQVSVGL YTSLCQYFSE EDMVWRTEGL LPLEETSPRQ AVCLTRHLTA FGASLFVPPS
HVRFVFPEPT ADVNYIVMLT CAVCLVTYMV MAAILHKLDQ LDASRGRAIP FCGQRGRFKY
EILVKTGWGR GSGTTAHVGI MLYGVDSRSG HRHLDGDRAF HRNSLDIFRI ATPHSLGSVW
KIRVWHDNKG LSPAWFLQHV IVRDLQTARS AFFLVNDWLS VETEANGGLV EKEVLAASDA
ALLRFRRLLV AELQRGFFDK HIWLSIWDRP PRSRFTRIQR ATCCVLLICL FLGANAVWYG
AVGDSAYSTG HVSRLSPLSV DTVAVGLVSS VVVYPVYLAI LFLFRMSRSK VAGSPSPTPA
GQQVLDIDSC LDSSVLDSSF LTFSGLHAEQ AFVGQMKSDL FLDDSKSLVC WPSGEGTLSW
PDLLSDPSIV GSNLRQLARG QAGHGLGPEE DGFSLASPYS PAKSFSASDE DLIQQVLAEG
VSSPAPTQDT HMETDLLSSL SSTPGEKTET LALQRLGELG PPSPGLNWEQ PQAARLSRTG
LVEGLRKRLL PAWCASLAHG LSLLLVAVAV AVSGWVGASF PPGVSVAWLL SSSASFLASF
LGWEPLKVLL EALYFSLVAK RLHPDEDDTL VESPAVTPVS ARVPRVRPPH GFALFLAKEE
ARKVKRLHGM LRSLLVYMLF LLVTLLASYG DASCHGHAYR LQSAIKQELH SRAFLAITRS
EELWPWMAHV LLPYVHGNQS SPELGPPRLR QVRLQEALYP DPPGPRVHTC SAAGGFSTSD
YDVGWESPHN GSGTWAYSAP DLLGAWSWGS CAVYDSGGYV QELGLSLEES RDRLRFLQLH
NWLDNRSRAV FLELTRYSPA VGLHAAVTLR LEFPAAGRAL AALSVRPFAL RRLSAGLSLP
LLTSVCLLLF AVHFAVAEAR TWHREGRWRV LRLGAWARWL LVALTAATAL VRLAQLGAAD
RQWTRFVRGR PRRFTSFDQV AQLSSAARGL AASLLFLLLV KAAQQLRFVR QWSVFGKTLC
RALPELLGVT LGLVVLGVAY AQLAILLVSS CVDSLWSVAQ ALLVLCPGTG LSTLCPAESW
HLSPLLCVGL WALRLWGALR LGAVILRWRY HALRGELYRP AWEPQDYEMV ELFLRRLRLW
MGLSKVKEFR HKVRFEGMEP LPSRSSRGSK VSPDVPPPSA GSDASHPSTS SSQLDGLSVS
LGRLGTRCEP EPSRLQAVFE ALLTQFDRLN QATEDVYQLE QQLHSLQGRR SSRAPAGSSR
GPSPGLRPAL PSRLARASRG VDLATGPSRT PLRAKNKVHP SST
