ID PKD1_MOUSE Reviewed; 4293 AA.
AC O08852; E9QJR6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 181.
DE RecName: Full=Polycystin-1 {ECO:0000305};
DE AltName: Full=Autosomal dominant polycystic kidney disease 1 protein homolog;
DE Flags: Precursor;
GN Name=Pkd1 {ECO:0000312|MGI:MGI:97603};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9107672; DOI=10.1007/s003359900429;
RA Lohning C., Nowicka U., Frischauf A.M.;
RT "The mouse homolog of PKD1: sequence analysis and alternative splicing.";
RL Mamm. Genome 8:307-311(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12514735; DOI=10.1038/ng1076;
RA Nauli S.M., Alenghat F.J., Luo Y., Williams E., Vassilev P., Li X.,
RA Elia A.E., Lu W., Brown E.M., Quinn S.J., Ingber D.E., Zhou J.;
RT "Polycystins 1 and 2 mediate mechanosensation in the primary cilium of
RT kidney cells.";
RL Nat. Genet. 33:129-137(2003).
RN [4]
RP INTERACTION WITH PKD2L1.
RX PubMed=15548533; DOI=10.1074/jbc.m411496200;
RA Murakami M., Ohba T., Xu F., Shida S., Satoh E., Ono K., Miyoshi I.,
RA Watanabe H., Ito H., Iijima T.;
RT "Genomic organization and functional analysis of murine PKD2L1.";
RL J. Biol. Chem. 280:5626-5635(2005).
RN [5]
RP DISRUPTION PHENOTYPE, AND DIFFERENTIAL PATTERN OF AUTOCLEAVAGE.
RX PubMed=18003909; DOI=10.1073/pnas.0708217104;
RA Yu S., Hackmann K., Gao J., He X., Piontek K., Garcia-Gonzalez M.A.,
RA Menezes L.F., Xu H., Germino G.G., Zuo J., Qian F.;
RT "Essential role of cleavage of Polycystin-1 at G protein-coupled receptor
RT proteolytic site for kidney tubular structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18688-18693(2007).
RN [6]
RP FUNCTION AS REGULATOR OF CILIUM LENGTH.
RX PubMed=20096584; DOI=10.1016/j.cub.2009.11.072;
RA Besschetnova T.Y., Kolpakova-Hart E., Guan Y., Zhou J., Olsen B.R.,
RA Shah J.V.;
RT "Identification of signaling pathways regulating primary cilium length and
RT flow-mediated adaptation.";
RL Curr. Biol. 20:182-187(2010).
RN [7]
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH PKD2 AND RABEP1, AND AUTOCATALYTIC
RP CLEAVAGE.
RX PubMed=25405894; DOI=10.1038/ncomms6482;
RA Kim H., Xu H., Yao Q., Li W., Huang Q., Outeda P., Cebotaru V.,
RA Chiaravalli M., Boletta A., Piontek K., Germino G.G., Weinman E.J.,
RA Watnick T., Qian F.;
RT "Ciliary membrane proteins traffic through the Golgi via a
RT Rabep1/GGA1/Arl3-dependent mechanism.";
RL Nat. Commun. 5:5482-5482(2014).
RN [10]
RP INTERACTION WITH WNT5A; DVL1 AND DVL2.
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).
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. Both PKD1 and PKD2
CC are required for channel activity (By similarity). Involved in renal
CC tubulogenesis (PubMed:24939912). Involved in fluid-flow
CC mechanosensation by the primary cilium in renal epithelium
CC (PubMed:12514735). Acts as a regulator of cilium length, together with
CC PKD2 (PubMed:20096584). The dynamic control of cilium length is
CC essential in the regulation of mechanotransductive signaling. 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. May be an ion-channel regulator. Involved in
CC adhesive protein-protein and protein-carbohydrate interactions. Likely
CC to be involved with polycystin-1-interacting protein 1 in the
CC detection, sequestration and exocytosis of senescent mitochondria (By
CC similarity). {ECO:0000250|UniProtKB:P98161,
CC ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:20096584,
CC ECO:0000269|PubMed:24939912}.
CC -!- SUBUNIT: Component of the heterotetrameric polycystin channel complex
CC with PKD2; the tetramer contains one PKD1 chain and three PKD2 chains
CC (By similarity). Interacts with PKD2; the interaction is required for
CC ciliary localization (PubMed:25405894). Interacts with PKD2L1
CC (PubMed:15548533). Interacts with PRKX; involved in differentiation and
CC controlled morphogenesis of the kidney. Interacts (via extracellular
CC domain) with WNT3A, WNT4 and WNT9B (By similarity). Interacts with
CC WNT5A, DVL1 and DVL2 (PubMed:27214281). Interacts with NPHP1 (via SH3
CC domain) (PubMed:20856870). Interacts with BBS1, BBS4, BBS5 and TTC8.
CC Interacts with RGS7 (By similarity). Interacts (via C-terminal domain)
CC with RABEP1; the interaction connects PKD1:PKD2 to GGA1 and ARL3 that
CC mediate the ciliary targeting (PubMed:25405894). Interacts (via the PKD
CC repeats in the N-terminal extracellular region) with EPCIP; the
CC interaction is not dependent on N-glycosylation of either protein (By
CC similarity). {ECO:0000250|UniProtKB:P98161,
CC ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:20856870,
CC ECO:0000269|PubMed:25405894, ECO:0000269|PubMed:27214281}.
CC -!- INTERACTION:
CC O08852; Q13563-1: PKD2; Xeno; NbExp=2; IntAct=EBI-6666305, EBI-9837017;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P98161};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P98161}. Cell
CC projection, cilium {ECO:0000269|PubMed:12514735,
CC ECO:0000269|PubMed:24939912, ECO:0000269|PubMed:25405894}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:25405894}. Golgi apparatus
CC {ECO:0000269|PubMed:25405894}. Vesicle {ECO:0000250|UniProtKB:P98161}.
CC Secreted, extracellular exosome {ECO:0000250|UniProtKB:P98161}.
CC Note=PKD1 localization to the plasma and ciliary membranes requires
CC PKD2, is independent of PKD2 channel activity, and involves stimulation
CC of PKD1 autocatalytic cleavage at the GPS domain (PubMed:12514735,
CC PubMed:25405894). PKD1:PKD2 interaction is required to reach the Golgi
CC apparatus from endoplasmic reticulum and then traffic to the cilia
CC (PubMed:25405894). Ciliary localization of PKD1 requires BBS1 and
CC ARL6/BBS3 (PubMed:24939912). Cell surface localization requires GANAB
CC (By similarity). Detected on migrasomes and on extracellular exosomes
CC in urine (By similarity). {ECO:0000250|UniProtKB:P98161,
CC ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:24939912,
CC ECO:0000269|PubMed:25405894}.
CC -!- DOMAIN: The LDL-receptor class A domain is atypical; the potential
CC calcium-binding site is missing.
CC -!- PTM: After synthesis, undergoes autoproteolytic cleavage between Leu-
CC 3040 and Thr-3041 in the GPS domain (PubMed:25405894). Cleavage at the
CC GPS domain occurs through a cis-autoproteolytic mechanism involving an
CC ester-intermediate via N-O acyl rearrangement (By similarity). This
CC process takes place in the early secretory pathway, depends on initial
CC N-glycosylation, and requires the REJ domain (By similarity). PKD1 is
CC ubiquitously and incompletely cleaved in wild-type mice, so that
CC uncleaved and cleaved PKD1 molecules coexist. The differential patterns
CC of cleavage during embryonic development, as well as in adult mice,
CC suggest different functions of uncleaved and cleaved molecules
CC (PubMed:18003909). {ECO:0000250|UniProtKB:P98161,
CC ECO:0000269|PubMed:18003909, ECO:0000269|PubMed:25405894}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P98161}.
CC -!- DISRUPTION PHENOTYPE: Knockin mice expressing non-cleavable PKD1 show a
CC hypomorphic phenotype. They are viable, show rapid cystic dilation in
CC renal collecting duct and distal convoluted tubule, but not in the
CC proximal portion of the nephron, during the postnatal period, and die
CC with severe uremia, mostly at 3 weeks of age. Additionally, they show
CC dilation of the common bile duct and intrahepatic biliary ducts, but
CC develop a normal pancreas within their life span.
CC {ECO:0000269|PubMed:18003909}.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
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_mou_Ctlect_149";
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DR EMBL; U70209; AAC53207.1; -; mRNA.
DR EMBL; AC132367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS28485.1; -.
DR RefSeq; NP_038658.2; NM_013630.2.
DR SMR; O08852; -.
DR BioGRID; 202204; 3.
DR ComplexPortal; CPX-4041; PKD1-PKD2 Polycystin complex.
DR DIP; DIP-44233N; -.
DR IntAct; O08852; 8.
DR MINT; O08852; -.
DR STRING; 10090.ENSMUSP00000049296; -.
DR MEROPS; P02.036; -.
DR GlyCosmos; O08852; 63 sites, No reported glycans.
DR GlyGen; O08852; 63 sites.
DR iPTMnet; O08852; -.
DR PhosphoSitePlus; O08852; -.
DR SwissPalm; O08852; -.
DR MaxQB; O08852; -.
DR PaxDb; 10090-ENSMUSP00000049296; -.
DR ProteomicsDB; 289438; -.
DR Pumba; O08852; -.
DR Antibodypedia; 23502; 254 antibodies from 29 providers.
DR DNASU; 18763; -.
DR Ensembl; ENSMUST00000035565.5; ENSMUSP00000049296.4; ENSMUSG00000032855.7.
DR GeneID; 18763; -.
DR KEGG; mmu:18763; -.
DR UCSC; uc008awv.1; mouse.
DR AGR; MGI:97603; -.
DR CTD; 5310; -.
DR MGI; MGI:97603; Pkd1.
DR VEuPathDB; HostDB:ENSMUSG00000032855; -.
DR eggNOG; KOG3599; Eukaryota.
DR GeneTree; ENSGT00940000158702; -.
DR HOGENOM; CLU_000173_0_0_1; -.
DR InParanoid; O08852; -.
DR OMA; WETPEPF; -.
DR OrthoDB; 52189at2759; -.
DR PhylomeDB; O08852; -.
DR TreeFam; TF316484; -.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 18763; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Pkd1; mouse.
DR PRO; PR:O08852; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O08852; Protein.
DR Bgee; ENSMUSG00000032855; Expressed in cerebellar cortex and 139 other cell types or tissues.
DR ExpressionAtlas; O08852; baseline and differential.
DR Genevisible; O08852; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0034704; C:calcium channel complex; ISO:MGI.
DR GO; GO:0034703; C:cation channel complex; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IMP:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0140494; C:migrasome; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0002133; C:polycystin complex; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IMP:BHF-UCL.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005261; F:monoatomic cation channel activity; IPI:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IMP:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0042813; F:Wnt receptor activity; ISO:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:BHF-UCL.
DR GO; GO:0006816; P:calcium ion transport; IDA:ComplexPortal.
DR GO; GO:0001502; P:cartilage condensation; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0198738; P:cell-cell signaling by wnt; ISO:MGI.
DR GO; GO:0050982; P:detection of mechanical stimulus; IDA:MGI.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0001892; P:embryonic placenta development; IMP:BHF-UCL.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IMP:MGI.
DR GO; GO:0048806; P:genitalia development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:BHF-UCL.
DR GO; GO:0001889; P:liver development; IGI:MGI.
DR GO; GO:0060428; P:lung epithelium development; IEA:Ensembl.
DR GO; GO:0036303; P:lymph vessel morphogenesis; IMP:MGI.
DR GO; GO:0072177; P:mesonephric duct development; IEA:Ensembl.
DR GO; GO:0072218; P:metanephric ascending thin limb development; IEA:Ensembl.
DR GO; GO:0072205; P:metanephric collecting duct development; IEA:Ensembl.
DR GO; GO:0072287; P:metanephric distal tubule morphogenesis; IEA:Ensembl.
DR GO; GO:0072237; P:metanephric proximal tubule development; IEA:Ensembl.
DR GO; GO:0160040; P:mitocytosis; ISS:UniProtKB.
DR GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IGI:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0060674; P:placenta blood vessel development; IMP:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006611; P:protein export from nucleus; IMP:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:MGI.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:MGI.
DR GO; GO:0034405; P:response to fluid shear stress; IMP:MGI.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00146; PKD; 11.
DR CDD; cd01752; PLAT_polycystin; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; IPR046791; Polycystin_dom.
DR InterPro; IPR014010; REJ_dom.
DR InterPro; IPR002889; WSC_carb-bd.
DR NCBIfam; TIGR00864; PCC; 1.
DR PANTHER; PTHR46730; POLYCYSTIN-1; 1.
DR PANTHER; PTHR46730:SF3; POLYCYSTIN-1; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00801; PKD; 14.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF20519; Polycystin_dom; 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; 1.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SMART; SM00089; PKD; 15.
DR SMART; SM00321; WSC; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF49299; PKD domain; 13.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS51450; LRR; 3.
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 Autocatalytic cleavage; Cell membrane; Cell projection; Cilium;
KW Coiled coil; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Lectin; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..4293
FT /note="Polycystin-1"
FT /id="PRO_0000354054"
FT TOPO_DOM 24..3066
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 3067..3087
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P98161"
FT TOPO_DOM 3088..3269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3270..3290
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P98161"
FT TOPO_DOM 3291..3315
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 3316..3336
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P98161"
FT TOPO_DOM 3337..3549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3550..3570
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P98161"
FT TOPO_DOM 3571..3572
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 3573..3593
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P98161"
FT TOPO_DOM 3594..3655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3656..3676
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P98161"
FT TOPO_DOM 3677..3891
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 3892..3912
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P98161"
FT TOPO_DOM 3913..3925
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3926..3946
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P98161"
FT TOPO_DOM 3947..3974
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 3975..3995
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P98161"
FT TOPO_DOM 3996..4017
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4018..4038
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P98161"
FT TOPO_DOM 4039..4080
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 4081..4100
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P98161"
FT TOPO_DOM 4101..4293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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..530
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 633..666
FT /note="LDL-receptor class A; atypical"
FT DOMAIN 849..922
FT /note="PKD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 929..1014
FT /note="PKD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1017..1123
FT /note="PKD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1121..1209
FT /note="PKD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1207..1292
FT /note="PKD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1288..1377
FT /note="PKD 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1376..1463
FT /note="PKD 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1462..1545
FT /note="PKD 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1544..1629
FT /note="PKD 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1630..1718
FT /note="PKD 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1716..1802
FT /note="PKD 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1804..1886
FT /note="PKD 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1885..1970
FT /note="PKD 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 1972..2053
FT /note="PKD 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 2056..2144
FT /note="PKD 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 2142..2828
FT /note="REJ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00511"
FT DOMAIN 3004..3053
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT DOMAIN 3110..3225
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 613..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4150..4197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4235..4293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4210..4241
FT /evidence="ECO:0000255"
FT COMPBIAS 4154..4197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4261..4293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 3040..3041
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT MOD_RES 4156
FT /note="Phosphoserine; by PRKX; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P98161"
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 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 848
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 859
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 884
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 998
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 1028
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1084
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1096
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1831
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1863
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1876
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1987
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2046
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2836
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2873
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3728
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 436..529
FT /evidence="ECO:0000250"
FT DISULFID 507..521
FT /evidence="ECO:0000250"
FT DISULFID 635..648
FT /evidence="ECO:0000250"
FT DISULFID 642..660
FT /evidence="ECO:0000250"
FT CONFLICT 3
FT /note="L -> P (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="R -> Q (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="E -> D (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 1180
FT /note="A -> T (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 1292
FT /note="H -> R (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 1632
FT /note="A -> V (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 1684
FT /note="S -> A (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 1770
FT /note="A -> T (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 2085
FT /note="R -> C (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 2507
FT /note="A -> V (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 3956
FT /note="F -> C (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 3962
FT /note="R -> H (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 4237
FT /note="Q -> R (in Ref. 1; AAC53207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4293 AA; 466577 MW; FA12403171DBBCE0 CRC64;
MPLGAPALLA LALGLGLWLG ALAGDPGRGC GPCPLPCFCG PAPDAACRVN CSGRWLQTLG
PSLRIPADAT ALDLSHNLLQ TLDIGLLVNL SALVELDLSN NRISTLEEGV FANLFNLSEI
NLSGNPFECN CGLAWLPRWA KEHQVHVVQS EATTCRGPIP LAGQPLLSIP LLDNACGEEY
VACLPDNSSG AVAAVPFYFA HEGPLETEAC SAFCFSAGEG LAALSEQNQC LCGAGQASNS
SAACSSWCSS ISLSLNSACG GPTLLQHTFP ASPGATLVGP HGPLASGQPA DFHITSSLPI
SSTRWNFGDG SPEVDMASPA ATHFYVLPGS YHMTVVLALG AGSALLETEV QVEATPTVLE
LVCPSFVHSN ESLELGIRHR GGSALEVTYS ILALDKEPAQ VVHPLCPLDT EIFPGNGHCY
RLVAEKAPWL QAQEQCRTWA GAALAMVDSP AIQHFLVSKV TRSLDVWIGF SSVEGTEGLD
PRGEAFSLES CQNWLPGEPH PATAEHCVRL GPAGQCNTDL CSAPHSYVCE LRPGGPVWDT
ENFVMGMSGG GLSGPLHPLA QQETVQGPLR PVEVMVFPGL SPSREAFLTA AEFSTQKLEE
PAQMRLQVYR PSGGAAAVPE GSSEPDNRTE PAPKCVPEEL WCPGANVCIP FDASCNSHVC
INGSVSRLGL SRASYTLWKE FFFSVPAGPP TQYLVTLHSQ DVPMLPGDLI GLQHDAGPGT
LLQCPLASSC PGQALYLSTN ASDWMTNLPV HLEEAWAGPV CSLQLLLVTE RLTPLLGLGP
NPGLQHPGHY EVRATVGNSV SRQNLSCSFS VVSPIAGLRV IHPIPLDGHI YVPTNGSVLV
LQVDSGANAT ATAQWFGGNI SAPFEDACPP EVDFLKQDCT EEANGTLFSV LMLPRLKEGD
HTVEIVAQNG ASQANLSLRV TAEEPICGLR AVPSPEARVL QGILVRYSPM VEAGSDVAFR
WTIDDKQSLT FHNTVFNVIY QSAAIFKLSL TASNHVSNIT VNYNVTVERM NKMHGLWVSA
VPTVLPPNAT LALTGGVLVD SAVEVAFLWN FGDGEQVLRQ FKPPYDESFQ VPDPTVAQVL
VEHNTTHIYT TPGEYNLTVL VSNTYENLTQ QVTVSVRTVL PNVAIGMSSN VLVAGQPITF
SPYPLPSTDG VLYTWDFGDG SPVLIQSQPV LNHTYSMTGA YRITLEVNNT VSSVTAHADI
RVFQELHGLT VYLSPSVEQG APMVVSASVE SGDNITWTFD MGDGTVFTGP EATVQHVYLR
AQNFTVTVEA ANPAGHLSQS LHVQVFVLEV LHIEPSTCIP TQPSAQLMAH VTGDPVHYLF
DWTFGDGSSN VTVHGHPSVT HNFTRSGIFP LALVLSSHVN KAHYFTSICV EPEIRNITLQ
PERQFVKLGD EARLVAYSWP PFPYRYTWDF GTEDTTHTQT GGSEVKFIYR EPGSYLVIVT
VSNNISSTND SAFVEVQEPV LVTGIRINGS HVLELQQPYL LSAMGSGSPA TYLWELGDGS
QSEGPEVTHI YSSTGDFTVR VSGWNEVSRS EAQLNITVKQ RVRGLTINAS RTVVPLNGSV
SFSTLLEVGS DVHYSWVLCD RCTPIPGGPT ISYTFRSVGT FNIIVTAENE VGSAQDSIFI
YVLQFIEGLQ VAGGDNGCCF PTNYTLQLQA AVRDGTNISY SWTAQQEGSL ITLFGSGKCF
SLTSLKASTY YVHLRATNML GSAAANRTID FVEPVESLIL SASPNPAAVN MSLTLCAELA
GGSGVVYTWY LEEGLSWKTS MPSTTHTFAA PGLHLVRVTA ENQLGSVNAT VEVAIQVPVG
GLSIRTSEPD SIFVAAGSTL PFWGQLAEGT NVTWCWTLPG GSKDSQYIAV RFSTAGSFSL
QLNASNAVSW VSAMYNLTVE EPIVNLMLWA SSKVVAPGQP VHFEILLAAG SALTFRLQVG
GSVPEVLPSP HFSHSFFRVG DHLVNVQAEN HVSHAQAQVR ILVLEAVVGL QVPNCCEPGM
ATGTEKNFTA RVQRGSRVAY AWYFSLQKVQ GDSLVILSGR DVTYTPVAAG LLEIHVRAFN
ELGGVNLTLM VEVQDIIQYV TLQSGRCFTN RSARFEAATS PSPRRVTYHW DFGDGTPVQK
TEEFWADHYY LRPGDYHVEV NATNLVSFFV AQATVTVQVL ACREPEVEVA LPLQVLMRRS
QRNYLEAHVD LRNCVSYQTE YRWEIYRTAS CQRPGRMAQM VLPGVDVSRP QLVVPRLALP
VGHYCFVFVV SFGDTPLARS IQANVTVAAE RLVPIIEGGS YRVWSDTQDL VLDGSKSYDP
NLEDGDQTPL NFHWACVAST QSETGGCVLN FGPRGSSVVT IPLERLEAGV EYTFNLIVWK
AGRKEEATNQ TVLIRSGRVP IVSLECVSCK AQAVYEVSRS SYVYLEGHCH NCSRGYKQGC
WAARTFSNKT LVLNETTTST GSTGMNLVVR PGALRDGEGY IFTLTVLGHS GEEEGCASIR
LSPNRPPLGG SCRLFPLDSV RGLTTKVHFE CTGWRDAEDG GAPLVYALLL KRCRQSYCEN
FCIYKGSLST YGAVLPPGFQ PLFVVSLAVV VQDQLGAAVV ALNRSLTIVL PEPSGNPADL
VPWLHSLTAS VLPGLLKQAD PQHVIEYSLA LITVLNEYEQ APDVSEPNVE QQLRAQMRKN
ITETLISLRV NTVDDIQQIT AALAQCMVSS RELMCRSCLK KMLQKLEGMM RILQAETTEG
TLTPTTIADS ILNITGDLIH LASLDMQGPQ PLELGVEPPS LMVASKAYNL SSALMRILMR
SRVLNEEPLT LAGEEIVALG KRSDPLSLLC YGKALGPSCH FSIPEAFSGA LSNLSDVVQL
IFLVDSNPFP FGYISNYTVS TKVASMAFQT QTGTQIPIEQ LAAERAITVK VPNNSDQAAQ
SSHNPVGSTI VQPQTSVSAV VTADNSNPQA GLHLRITYTV LNERYLSAEP EPYLAVYLHS
VSQPNEYNCS ASRRISLEVL EGADHRLYTF FIAPGTGTLD RSYYLNLTSH FHWSALEVSV
GLYTSLCQYF SEEMMMWRTE GIVPLEETSP SQAVCLTRHL TAFGASLFVP PSHVQFIFPE
PSASINYIVL LTCVICLVTY VVMAMILRKL DQLDVSRVRV IPFCGKGGRF KYEILVKTGW
SRGSGTTAHV GIMLYGEDNR SGHRHLDGDR AFHRNSLDIF QIATPHSLGS VWKIRVWHDN
KGLSPAWFLQ HIIVRDLQSA RSTFFLVNDW LSVETEANGG LVEKEVLAAN EAALWQFQRL
LVAELQRGFF DKHIWLSIWD RPPRSRFTRV QRVTCCVLLL CLFLAANAVW YGVVRDTTYS
MGPVSSLISP GVDTVAIGLV SSVVVYPVYL AVLFLFRMSR SKVSGDQNPT PTGQQALDVD
SYLDPSVLDS SLLTLSGLTE AFAGQVKNDL FLEDAKSLVC WPSSEGTLSW PDLLSDPSVV
SSTLQRLTQG RPGCMLGSEE DGASLVSPSL PAKYLSASDE DLIHQVLADG ANNLVPTQDT
LLETDLLTSL SSVPGEKTET LILQTVGEER PASMGLSWEQ SPVTRLSRTG LVEGFQKRLL
PAWCAPLAHG LSLLLVAVAV AVSGWIGASF PPSVSVMWLL SSSSSFLASF LGWEPLKVLL
EALYFSLVAK RLHPDEDDTL VESPAVTPVS ERVPRVRPPH GFALFLAKEE ARKVKRLHDM
LKRLLVYMLF LLVTLLANYG DASCHGHAYR LQSAIKQELD SQAFLAITRS DEFWPWMSHV
FLPYVHGNQS SPELGPPRLR QVRLQEAFCP DPSSSEHMCS AAGSLSTSDY GIGWQSVVQN
GSETWAYSAP DLLGAWYWGY CAVYDSGGYI QELGLSLEES RARLGFLQLH NWLDSRSRAV
FVELTRYSPA VGLHAAVTLR LEFPVAGHAL AAFSVRPFAL RRLSTGLSLP LLTSVCLLLF
ALYFSMAEVQ TWRKDGCACT ARPDTWARCL LVILTAATGL VRLAQLGIAD RQWTHFVQDH
PRHFTSFDQV AQLGSVARGL AASLLFLLLV KAAQQLRFVR QWSVFGKTLC RALPELMGAT
LGLVLLGVAY AQMAILLISS GADTLYNMAR AFLVLCPGAR VPTLCPSESW YLSPLLCVGL
WALRVWGALR LGAILLRWRY HALRGELYRP AWEPQDYEMV ELFLRRLRLW MGFSKVKEFR
HKVRFEGMDP LPSRSSRGSK SSPVVLPPSS GSEASHPSTS SSQPDGPSAS LSRSTLKLEP
EPSRLHAVFE SLLVQFDRLN QATEDVYQLE QQLQSLQGHG HNGPPSSPSP GCFPGSQPAL
PSRLSRASQG LDQTVGPNRV SLWPNNKVHP SST
//
