| IED ID | IndEnz0009000312 |
| Enzyme Type ID | chitinase000312 |
| Protein Name |
Polycystin-1 PC1 Autosomal dominant polycystic kidney disease 1 protein |
| Gene Name | PKD1 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MPPAAPARLALALGLGLWLGALAGGPGRGCGPCEPPCLCGPAPGAACRVNCSGRGLRTLGPALRIPADATALDVSHNLLRALDVGLLANLSALAELDISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLAWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSGCGEEYVACLPDNSSGTVAAVSFSAAHEGLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSASFACLSLCSGPPPPPAPTCRGPTLLQHVFPASPGATLVGPHGPLASGQLAAFHIAAPLPVTATRWDFGDGSAEVDAAGPAASHRYVLPGRYHVTAVLALGAGSALLGTDVQVEAAPAALELVCPSSVQSDESLDLSIQNRGGSGLEAAYSIVALGEEPARAVHPLCPSDTEIFPGNGHCYRLVVEKAAWLQAQEQCQAWAGAALAMVDSPAVQRFLVSRVTRSLDVWIGFSTVQGVEVGPAPQGEAFSLESCQNWLPGEPHPATAEHCVRLGPTGWCNTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLAQQDGLSAPHEPVEVMVFPGLRLSREAFLTTAEFGTQELRRPAQLRLQVYRLLSTAGTPENGSEPESRSPDNRTQLAPACMPGGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAPYALWREFLFSVPAGPPAQYSVTLHGQDVLMLPGDLVGLQHDAGPGALLHCSPAPGHPGPRAPYLSANASSWLPHLPAQLEGTWACPACALRLLAATEQLTVLLGLRPNPGLRLPGRYEVRAEVGNGVSRHNLSCSFDVVSPVAGLRVIYPAPRDGRLYVPTNGSALVLQVDSGANATATARWPGGSVSARFENVCPALVATFVPGCPWETNDTLFSVVALPWLSEGEHVVDVVVENSASRANLSLRVTAEEPICGLRATPSPEARVLQGVLVRYSPVVEAGSDMVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSLTASNHVSNVTVNYNVTVERMNRMQGLQVSTVPAVLSPNATLALTAGVLVDSAVEVAFLWTFGDGEQALHQFQPPYNESFPVPDPSVAQVLVEHNVMHTYAAPGEYLLTVLASNAFENLTQQVPVSVRASLPSVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLYTWDFGDGSPVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVRVFEELRGLSVDMSLAVEQGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVLRVEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAHYFTSICVEPEVGNVTLQPERQFVQLGDEAWLVACAWPPFPYRYTWDFGTEEAAPTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEVQEPVLVTSIKVNGSLGLELQQPYLFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVKRRVRGLVVNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYVLQLIEGLQVVGGGRYFPTNHTVQLQAVVRDGTNVSYSWTAWRDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTMTAGNPLGSANATVEVDVQVPVSGLSIRASEPGGSFVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSATYNLTAEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGANPEVLPGPRFSHSFPRVGDHVVSVRGKNHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARVQRGSRVAYAWYFSLQKVQGDSLVILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALQSGPCFTNRSAQFEAATSPSPRRVAYHWDFGDGSPGQDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVVLPLQVLMRRSQRNYLEAHVDLRDCVTYQTEYRWEVYRTASCQRPGRPARVALPGVDVSRPRLVLPRLALPVGHYCFVFVVSFGDTPLTQSIQANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVASTQREAGGCALNFGPRGSSTVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGRCLNCSSGSKRGRWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRPPLGGSCRLFPLGAVHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFCVYKGSLSSYGAVLPPGFRPHFEVGLAVVVQDQLGAAVVALNRSLAITLPEPNGSATGLTVWLHGLTASVLPGLLRQADPQHVIEYSLALVTVLNEYERALDVAAEPKHERQHRAQIRKNITETLVSLRVHTVDDIQQIAAALAQCMGPSRELVCRSCLKQTLHKLEAMMLILQAETTAGTVTPTAIGDSILNITGDLIHLASSDVRAPQPSELGAESPSRMVASQAYNLTSALMRILMRSRVLNEEPLTLAGEEIVAQGKRSDPRSLLCYGGAPGPGCHFSIPEAFSGALANLSDVVQLIFLVDSNPFPFGYISNYTVSTKVASMAFQTQAGAQIPIERLASERAITVKVPNNSDWAARGHRSSANSANSVVVQPQASVGAVVTLDSSNPAAGLHLQLNYTLLDGHYLSEEPEPYLAVYLHSEPRPNEHNCSASRRIRPESLQGADHRPYTFFISPGSRDPAGSYHLNLSSHFRWSALQVSVGLYTSLCQYFSEEDMVWRTEGLLPLEETSPRQAVCLTRHLTAFGASLFVPPSHVRFVFPEPTADVNYIVMLTCAVCLVTYMVMAAILHKLDQLDASRGRAIPFCGQRGRFKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAWFLQHVIVRDLQTARSAFFLVNDWLSVETEANGGLVEKEVLAASDAALLRFRRLLVAELQRGFFDKHIWLSIWDRPPRSRFTRIQRATCCVLLICLFLGANAVWYGAVGDSAYSTGHVSRLSPLSVDTVAVGLVSSVVVYPVYLAILFLFRMSRSKVAGSPSPTPAGQQVLDIDSCLDSSVLDSSFLTFSGLHAEQAFVGQMKSDLFLDDSKSLVCWPSGEGTLSWPDLLSDPSIVGSNLRQLARGQAGHGLGPEEDGFSLASPYSPAKSFSASDEDLIQQVLAEGVSSPAPTQDTHMETDLLSSLSSTPGEKTETLALQRLGELGPPSPGLNWEQPQAARLSRTGLVEGLRKRLLPAWCASLAHGLSLLLVAVAVAVSGWVGASFPPGVSVAWLLSSSASFLASFLGWEPLKVLLEALYFSLVAKRLHPDEDDTLVESPAVTPVSARVPRVRPPHGFALFLAKEEARKVKRLHGMLRSLLVYMLFLLVTLLASYGDASCHGHAYRLQSAIKQELHSRAFLAITRSEELWPWMAHVLLPYVHGNQSSPELGPPRLRQVRLQEALYPDPPGPRVHTCSAAGGFSTSDYDVGWESPHNGSGTWAYSAPDLLGAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDNRSRAVFLELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALRRLSAGLSLPLLTSVCLLLFAVHFAVAEARTWHREGRWRVLRLGAWARWLLVALTAATALVRLAQLGAADRQWTRFVRGRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELLGVTLGLVVLGVAYAQLAILLVSSCVDSLWSVAQALLVLCPGTGLSTLCPAESWHLSPLLCVGLWALRLWGALRLGAVILRWRYHALRGELYRPAWEPQDYEMVELFLRRLRLWMGLSKVKEFRHKVRFEGMEPLPSRSSRGSKVSPDVPPPSAGSDASHPSTSSSQLDGLSVSLGRLGTRCEPEPSRLQAVFEALLTQFDRLNQATEDVYQLEQQLHSLQGRRSSRAPAGSSRGPSPGLRPALPSRLARASRGVDLATGPSRTPLRAKNKVHPSST |
| Enzyme Length | 4303 |
| Uniprot Accession Number | P98161 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B (PubMed:27214281). Both PKD1 and PKD2 are required for channel activity (PubMed:27214281). Involved in renal tubulogenesis (PubMed:12482949). Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (By similarity). Acts as a regulator of cilium length, together with PKD2 (By similarity). The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling (By similarity). 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 (By similarity). May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate interactions. {ECO:0000250|UniProtKB:O08852, ECO:0000269|PubMed:12482949, ECO:0000269|PubMed:27214281}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (7); Chain (1); Coiled coil (1); Compositional bias (3); Disulfide bond (5); Domain (25); Glycosylation (60); Modified residue (1); Mutagenesis (2); Natural variant (186); Region (3); Repeat (2); Sequence conflict (21); Signal peptide (1); Site (1); Topological domain (12); Transmembrane (11) |
| Keywords | 3D-structure;Alternative splicing;Autocatalytic cleavage;Cell membrane;Cell projection;Ciliopathy;Cilium;Coiled coil;Disease variant;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Golgi apparatus;Lectin;Leucine-rich repeat;Membrane;Phosphoprotein;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix;Wnt signaling pathway |
| Interact With | O15259; Q13563; Q13563-1; Q13563; Q13563-1 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10339594, ECO:0000269|PubMed:20980620, ECO:0000269|PubMed:27214281, ECO:0000269|PubMed:27259053, ECO:0000269|PubMed:30093605}; Multi-pass membrane protein {ECO:0000269|PubMed:20980620, ECO:0000269|PubMed:30093605}. Cell projection, cilium {ECO:0000250|UniProtKB:O08852}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O08852}. Golgi apparatus {ECO:0000250|UniProtKB:O08852}. Note=PKD1 localization to the plasma and ciliary membranes requires PKD2, is independent of PKD2 channel activity, and involves stimulation of PKD1 autoproteolytic cleavage at the GPS domain. PKD1:PKD2 interaction is required to reach the Golgi apparatus from endoplasmic reticulum and then traffic to the cilia (By similarity). Ciliary localization of PKD1 requires BBS1 and ARL6/BBS3 (By similarity). Cell surface localization requires GANAB (PubMed:27259053). {ECO:0000250|UniProtKB:O08852, ECO:0000269|PubMed:27259053}. |
| Modified Residue | MOD_RES 4166; /note=Phosphoserine; by PRKX; in vitro; /evidence=ECO:0000269|PubMed:17980165 |
| Post Translational Modification | PTM: After synthesis, undergoes cleavage between Leu-3048 and Thr-3049 in the GPS domain. Cleavage at the GPS domain occurs through a cis-autoproteolytic mechanism involving an ester-intermediate via N-O acyl rearrangement. This process takes place in the early secretory pathway, depends on initial N-glycosylation, and requires the REJ domain. There is evidence that cleavage at GPS domain is incomplete. Uncleaved and cleaved products may have different functions in vivo. {ECO:0000269|PubMed:12482949}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | NMR spectroscopy (1); Electron microscopy (1) |
| Cross Reference PDB | 1B4R; 6A70; |
| Mapped Pubmed ID | 10097141; 10362514; 11106764; 11836366; 11891195; 11901144; 11912216; 11961010; 12048202; 12221131; 12819240; 12946628; 14596619; 14718571; 15001556; 15060061; 15087466; 15158452; 15231748; 15284290; 15382167; 15466861; 15728366; 15748886; 15780076; 15870383; 16014040; 16038619; 16038802; 16136078; 16155582; 16215947; 16311606; 16319969; 16431365; 16481400; 16537653; 16565258; 16651260; 16741147; 16767665; 16778383; 16782012; 16790429; 17007872; 17030804; 17090781; 17102641; 17396115; 17437137; 17437318; 17451746; 17474147; 17540339; 17574030; 17574468; 17628206; 17646400; 17671167; 17890878; 18060739; 18263686; 18289888; 18298949; 18422703; 18566106; 18632682; 18685082; 18791038; 18922886; 19017632; 19153612; 19158352; 19158373; 19165178; 19194729; 19285554; 19297529; 19331813; 19443633; 19454479; 19686598; 19759016; 19854836; 20083215; 20168298; 20169078; 20201926; 20206434; 20219615; 20308558; 20388565; 20444281; 20557879; 20558538; 20674666; 20837139; 20923779; 20937836; 21048031; 21076887; 21126580; 21142036; 21273506; 21314639; 21332816; 21550243; 21565611; 21694639; 21775626; 21865467; 21867693; 21983717; 21998636; 22031115; 22034075; 22034641; 22227580; 22237240; 22367170; 22389062; 22409330; 22420621; 22426824; 22433857; 22456092; 22570239; 22582392; 22675472; 22872635; 22983554; 23001567; 23014991; 23028574; 23129748; 23300259; 23351793; 23390129; 23431072; 23431742; 23439951; 23475492; 23496908; 23567275; 23567335; 23624871; 23848298; 23850273; 23945166; 23985799; 24009235; 24153433; 24189120; 24193408; 24296415; 24385601; 24416790; 24491980; 24575920; 24683199; 24694054; 24707946; 24740233; 24821069; 24907393; 24925719; 25111597; 25123959; 25128071; 25180832; 25203322; 25287328; 25355409; 25365220; 25367197; 25491204; 25517939; 25531466; 25741140; 25757501; 25880449; 26096820; 26139440; 26632257; 26764245; 26775353; 26823553; 26932689; 26950445; 26984954; 26991955; 27179075; 27499327; 27567292; 27577987; 27699453; 27775029; 27782177; 27785750; 27835667; 27984604; 28076932; 28077787; 28154010; 28228588; 28375157; 28552828; 28578020; 28604956; 28620080; 28825164; 28827396; 28870863; 28904368; 28983800; 29034881; 29380239; 29465084; 29472562; 29529603; 29590654; 29633482; 29860066; 29896735; 29931260; 29973168; 30077613; 30101477; 30185468; 30230107; 30333007; 30388220; 30419840; 30424739; 30540438; 30816285; 30858458; 30895336; 31052533; 31079206; 31088850; 31167779; 31176519; 31251475; 31591827; 31740684; 31862184; 32001768; 32166738; 32171525; 32475690; 32505451; 32663194; 32724471; 32799769; 32816041; 32823016; 32970388; 32985371; 33111320; 33164752; 33602752; 33656806; 33939064; 33964006; 33994377; 34064452; 34175641; 34324862; 34858418; 34962918; 9211343; 9819391; |
| Motif | |
| Gene Encoded By | |
| Mass | 462,529 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |