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"; 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; 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 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. DR Genevisible; O08852; MM. 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 //