Q92673B2RNX7Q92856SORL_HUMANSortilin-related receptorLow-density lipoprotein receptor relative with 11 ligand-binding repeatsLDLR relative with 11 ligand-binding repeatsLR11SorLA-1Sorting protein-related receptor containing LDLR class A repeatsSorLASORL1C11orf32Homo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoA novel mosaic protein containing LDL receptor elements is highly conserved in humans and chickens.NUCLEOTIDE SEQUENCE [MRNA]VARIANTS GLU-1074 AND ILE-1967TISSUE SPECIFICITYMolecular characterization of a novel human hybrid-type receptor that binds the alpha2-macroglobulin receptor-associated protein.NUCLEOTIDE SEQUENCE [MRNA]PROTEIN SEQUENCE OF 82-91; 114-121; 405-415 AND 2019-2030VARIANTS GLU-1074 AND ILE-1967TISSUE SPECIFICITYINTERACTION WITH LRPAP1Human chromosome 11 DNA sequence and analysis including novel gene identification.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]VARIANTS GLU-1074 AND ILE-1967The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]VARIANTS GLU-1074 AND ILE-1967Ectodomain shedding, translocation and synthesis of SorLA are stimulated by its ligand head activator.INTERACTION WITH HAINDUCTION BY HASUBCELLULAR LOCATIONCLEAVAGE OF THE PROPEPTIDEActivation and functional characterization of the mosaic receptor SorLA/LR11.PROTEIN SEQUENCE OF 82-86CLEAVAGE OF THE PROPEPTIDEINTERACTION WITH HA; LRPAP1; NTS AND PROPEPTIDESUBCELLULAR LOCATIONGLYCOSYLATIONMUTAGENESIS OF 78-ARG--ARG-81Characterization of the VPS10 domain of SorLA/LR11 as binding site for the neuropeptide HA.INTERACTION WITH HA; LRPAP1 AND PROPEPTIDEThe sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding.INTERACTION WITH GGA1 AND GGA2The mosaic receptor sorLA/LR11 binds components of the plasminogen-activating system and platelet-derived growth factor-BB similarly to LRP1 (low-density lipoprotein receptor-related protein), but mediates slow internalization of bound ligand.SUBCELLULAR LOCATIONINTERACTION WITH LRPAP1; PDGFB; PLAT; PLAU AND SERPINE1LR11, an LDL receptor gene family member, is a novel regulator of smooth muscle cell migration.FUNCTIONSUBCELLULAR LOCATIONINTERACTION WITH PLAURFunctional organization of the sortilin Vps10p domain.INTERACTION WITH LRPAP1; GDNF AND PROPEPTIDENeuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein.FUNCTION IN APP TRAFFICKINGSUBCELLULAR LOCATIONINTERACTION WITH APPTISSUE SPECIFICITYTumour necrosis factor alpha-converting enzyme mediates ectodomain shedding of Vps10p-domain receptor family members.INTERACTION WITH PDGFBSUBCELLULAR LOCATIONSHEDDING BY ADAM17SorLA signaling by regulated intramembrane proteolysis.SUBCELLULAR LOCATIONCLEAVAGE BY PSEN1MUTAGENESIS OF 2163-ARG-ARG-2164Interaction of the cytosolic domains of sorLA/LR11 with the amyloid precursor protein (APP) and beta-secretase beta-site APP-cleaving enzyme.FUNCTIONINTERACTION WITH APP AND BACE1Apolipoprotein A-V interaction with members of the low density lipoprotein receptor gene family.INTERACTION WITH APOA5SorLA/LR11 regulates processing of amyloid precursor protein via interaction with adaptors GGA and PACS-1.FUNCTIONINTERACTION WITH APP; GGA1 AND PACS1SUBCELLULAR LOCATIONMUTAGENESIS OF 2190-ASP--ASP-2198 AND 2208-ASP--MET-2211Sorting by the cytoplasmic domain of the amyloid precursor protein binding receptor SorLA.FUNCTIONINTERACTION WITH PACS1; AP-1 COMPLEX AND AP-2 COMPLEXSUBCELLULAR LOCATIONMUTAGENESIS OF 2172-PHE--TYR-2177; 2190-ASP--ALA-2214; 2190-ASP--ASP-2198; 2201-MET-ILE-2202 AND 2211-MET--ALA-2214Endocytosis of apolipoprotein A-V by members of the low density lipoprotein receptor and the VPS10p domain receptor families.FUNCTIONINTERACTION WITH APOA5No association of SORL1 SNPs with Alzheimer's disease.LACK OF ASSOCIATION WITH SUSCEPTIBILITY TO LATE-ONSET ALZHEIMER DISEASEGlycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-99; ASN-1733; ASN-2010; ASN-2076 AND ASN-2092SORLA/SORL1 functionally interacts with SPAK to control renal activation of Na(+)-K(+)-Cl(-) cotransporter 2.INTERACTION WITH STK39Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Meta-analysis of the association between variants in SORL1 and Alzheimer disease.INVOLVEMENT IN ADRho kinase II phosphorylation of the lipoprotein receptor LR11/SORLA alters amyloid-beta production.PHOSPHORYLATION AT SER-2206INTERACTION WITH ROCK2TISSUE SPECIFICITYSorting protein-related receptor SorLA controls regulated secretion of glial cell line-derived neurotrophic factor.FUNCTIONINTERACTION WITH GDNFSUBCELLULAR LOCATIONSorLA regulates the activity of lipoprotein lipase by intracellular trafficking.FUNCTIONINTERACTION WITH LPLSUBCELLULAR LOCATIONTISSUE SPECIFICITYMUTAGENESIS OF 2211-MET--ALA-2214SorLA controls neurotrophic activity by sorting of GDNF and its receptors GFRalpha1 and RET.FUNCTIONINTERACTION WITH GDNF; GFRA1; GFRA2; GFRA3 AND GFRA4SUBCELLULAR LOCATIONThe soluble form of LR11 protein is a regulator of hypoxia-induced, urokinase-type plasminogen activator receptor (uPAR)-mediated adhesion of immature hematological cells.FUNCTIONINTERACTION WITH PLAURINDUCTION BY HYPOXIASORL1 is genetically associated with late-onset Alzheimer's disease in Japanese, Koreans and Caucasians.INVOLVEMENT IN ADSORLA-mediated trafficking of TrkB enhances the response of neurons to BDNF.FUNCTIONAn enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Lysosomal sorting of amyloid-beta by the SORLA receptor is impaired by a familial Alzheimer's disease mutation.FUNCTIONINTERACTION WITH APP AND PROPEPTIDECHARACTERIZATION OF VARIANT AD ARG-511Soluble LR11/SorLA represses thermogenesis in adipose tissue and correlates with BMI in humans.POTENTIAL ASSOCIATION WITH BODY MASS INDEXSORLA facilitates insulin receptor signaling in adipocytes and exacerbates obesity.FUNCTIONINTERACTION WITH INSRPOTENTIAL ASSOCIATION WITH BODY MASS INDEXCytokine-like factor 1, an essential facilitator of cardiotrophin-like cytokine:ciliary neurotrophic factor receptor alpha signaling and sorLA-mediated turnover.FUNCTIONINTERACTION WITH CLCF1; CRLF1; CNTFR AND LRPAP1SorLA in Interleukin-6 Signaling and Turnover.FUNCTIONINTERACTION WITH IL6 AND IL6RSHEDDING FROM THE CELL SURFACESoluble LR11 competes with amyloid beta in binding to cerebrospinal fluid-high-density lipoprotein.INTERACTION WITH APOESORLA regulates endosomal trafficking and oncogenic fitness of HER2.FUNCTIONINTERACTION WITH ERBB2SUBCELLULAR LOCATIONHSPA12A targets the cytoplasmic domain and affects the trafficking of the Amyloid Precursor Protein receptor SorLA.INTERACTION WITH GGA1 AND HSPA12AMUTAGENESIS OF 2190-ASP-ASP-2191; 2194-GLU--ASP-2198; 2203-THR-GLY-2204; 2205-PHE-SER-2206; 2207-ASP-ASP-2208 AND 2209-VAL-PRO-2210Solution structure of the second FN3 domain of human SORLA/LR11.STRUCTURE BY NMR OF 1651-1745GGA autoinhibition revisited.X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2202-2214 IN COMPLEX WITH GGA1INTERACTION WITH GGA1The consensus coding sequences of human breast and colorectal cancers.VARIANTS [LARGE SCALE ANALYSIS] SER-120; LEU-1581 AND VAL-1972SORL1 is genetically associated with increased risk for late-onset Alzheimer disease in the Belgian population.POSSIBLE ASSOCIATION WITH SUSCEPTIBILITY TO LATE-ONSET ALZHEIMER DISEASEVARIANT THR-528High frequency of potentially pathogenic SORL1 mutations in autosomal dominant early-onset Alzheimer disease.VARIANTS AD CYS-141; ARG-511; SER-924; SER-1358 AND ASP-1681Sorting receptor that directs several proteins to their correct location within the cell (Probable). Along with AP-1 complex, involved Golgi apparatus - endosome sorting (PubMed:17646382). Sorting receptor for APP, regulating its intracellular trafficking and processing into amyloidogenic-beta peptides. Retains APP in the trans-Golgi network, hence preventing its transit through late endosomes where amyloid beta peptides Abeta40 and Abeta42 are generated (PubMed:16174740, PubMed:16407538, PubMed:17855360, PubMed:24523320). May also sort newly produced amyloid-beta peptides to lysosomes for catabolism (PubMed:24523320). Does not affect APP trafficking from the endoplasmic reticulum to Golgi compartments (PubMed:17855360). Sorting receptor for the BDNF receptor NTRK2/TRKB that facilitates NTRK2 trafficking between synaptic plasma membranes, postsynaptic densities and cell soma, hence positively regulates BDNF signaling by controlling the intracellular location of its receptor (PubMed:23977241). Sorting receptor for GDNF that promotes GDNF regulated, but not constitutive secretion (PubMed:21994944). Sorting receptor for the GDNF-GFRA1 complex, directing it from the cell surface to endosomes. GDNF is then targeted to lysosomes and degraded, while its receptor GFRA1 recycles back to the cell membrane, resulting in a GDNF clearance pathway. The SORL1-GFRA1 complex further targets RET for endocytosis, but not for degradation, affecting GDNF-induced neurotrophic activities (PubMed:23333276). Sorting receptor for ERBB2/HER2. Regulates ERBB2 subcellular distribution by promoting its recycling after internalization from endosomes back to the plasma membrane, hence stimulating phosphoinositide 3-kinase (PI3K)-dependent ERBB2 signaling. In ERBB2-dependent cancer cells, promotes cell proliferation (PubMed:31138794). Sorting receptor for lipoprotein lipase LPL. Promotes LPL localization to endosomes and later to the lysosomes, leading to degradation of newly synthesized LPL (PubMed:21385844). Potential sorting receptor for APOA5, inducing APOA5 internalization to early endosomes, then to late endosomes, wherefrom a portion is sent to lysosomes and degradation, another portion is sorted to the trans-Golgi network (PubMed:18603531). Sorting receptor for the insulin receptor INSR. Promotes recycling of internalized INSR via the Golgi apparatus back to the cell surface, thereby preventing lysosomal INSR catabolism, increasing INSR cell surface expression and strengthening insulin signal reception in adipose tissue. Does not affect INSR internalization (PubMed:27322061). Plays a role in renal ion homeostasis, controlling the phospho-regulation of SLC12A1/NKCC2 by STK39/SPAK kinase and PPP3CB/calcineurin A beta phosphatase, possibly through intracellular sorting of STK39 and PPP3CB (By similarity). Stimulates, via the N-terminal ectodomain, the proliferation and migration of smooth muscle cells, possibly by increasing cell surface expression of the urokinase receptor uPAR/PLAUR. This may promote extracellular matrix proteolysis and hence facilitate cell migration (PubMed:14764453). By acting on the migration of intimal smooth muscle cells, may accelerate intimal thickening following vascular injury (PubMed:14764453). Promotes adhesion of monocytes (PubMed:23486467). Stimulates proliferation and migration of monocytes/macrophages (By similarity). Through its action on intimal smooth muscle cells and macrophages, may accelerate intimal thickening and macrophage foam cell formation in the process of atherosclerosis (By similarity). Regulates hypoxia-enhanced adhesion of hematopoietic stem and progenitor cells to the bone marrow stromal cells via a PLAUR-mediated pathway. This function is mediated by the N-terminal ectodomain (PubMed:23486467). Metabolic regulator, which functions to maintain the adequate balance between lipid storage and oxidation in response to changing environmental conditions, such as temperature and diet. The N-terminal ectodomain negatively regulates adipose tissue energy expenditure, acting through the inhibition the BMP/Smad pathway (By similarity). May regulate signaling by the heterodimeric neurotrophic cytokine CLCF1-CRLF1 bound to the CNTFR receptor by promoting the endocytosis of the tripartite complex CLCF1-CRLF1-CNTFR and lysosomal degradation (PubMed:26858303). May regulate IL6 signaling, decreasing cis signaling, possibly by interfering with IL6-binding to membrane-bound IL6R, while up-regulating trans signaling via soluble IL6R (PubMed:28265003).After maturation cleavage, interacts (via N-terminus) with its own propeptide; this interaction prevents interaction with other ligands, including CRLF1, GDNF, GFRA1, IL6 and IL6R (PubMed:11294867, PubMed:12530537, PubMed:15364913, PubMed:23333276, PubMed:24523320). Interacts (via N-terminal ectodomain) with APP, forming a 1:1 stoichiometric complex, including with isoforms APP695, APP751 and APP770; this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (PubMed:16174740, PubMed:16407538, PubMed:17855360, PubMed:24523320). Also interacts with APP C-terminal fragment C99 and with Abeta40 (PubMed:16407538). Interacts with beta-secretase BACE1/BACE; this interaction may affect BACE1-binding to APP and hence reduce BACE1-dependent APP cleavage (PubMed:16407538). Interacts with LRPAP1/RAP (PubMed:8940146, PubMed:11294867, PubMed:12530537, PubMed:15053742, PubMed:14764453, PubMed:15364913, PubMed:26858303). Interacts (via C-terminal cytosolic domain) with GGA1 and GGA2 (via N-terminal VHS domain) (PubMed:11821067, PubMed:17855360, PubMed:30679749, PubMed:20015111). Interacts with PACS1 (PubMed:17855360, PubMed:17646382). May interact (via the N-terminal ectodomain) with the morphogenetic neuropeptide, also called head activator or HA; this interaction is impaired in the presence of propeptide (PubMed:11082041, PubMed:11294867, PubMed:12530537). Interacts with neurotensin/NTS (PubMed:11294867). Interacts (via the N-terminal ectodomain) with PDGFB homodimer (PubMed:15053742, PubMed:16393139). Interacts (via N-terminal ectodomain) with the uPA receptor PLAUR; this interaction decreases PLAUR internalization (PubMed:14764453, PubMed:23486467). Interacts (via N-terminal ectodomain) with uPA/PLAU and PAI1/SERPINE1, either individually or in complex with each other, leading to endocytosis; this interaction is abolished in the presence of LRPAP1 (PubMed:15053742). Also interacts with the ternary complex composed of PLAUR-PLAU-PAI1 (PubMed:15053742). Also interacts with tPA/PLAT either alone or in complex with SERPINE1 (PubMed:15053742). Interacts (via C-terminus) with AP-1 and AP-2 complexes (PubMed:17646382). Interacts with BMPR1A and BMPR1B (By similarity). Interacts with lipoprotein lipase LPL; this interaction is optimal in slightly acidic conditions (PubMed:21385844). Interacts (via N-terminal ectodomain) with GDNF (via propeptide) and GDNF receptor alpha-1/GFRA1, either individually or in complex with each other (PubMed:15364913, PubMed:21994944, PubMed:23333276). The interaction with GDNF occurs mostly intracellularly (PubMed:21994944). Also interacts with other GDNF receptor alpha family members, including GFRA2, GFRA3 and GFRA4 (PubMed:23333276). Interacts with the insulin receptor INSR; this interaction strongly increases the surface exposure of INSR (PubMed:27322061). Interacts (via cytosolic C-terminus) with STK39/SPAK (PubMed:20385770). Interacts (via N-terminal ectodomain) with the heterodimeric complex CRLF1-CLC; within this complex, the interaction is mediated predominantly by the CRLF1 moiety (PubMed:26858303). Interacts with CNTFR, as well as with the tripartite signaling complex formed by CRLF1, CLC and CNTFR (PubMed:26858303). Interacts (via N-terminal ectodomain) with IL6; this interaction leads to IL6 internalization and lysosomal degradation (PubMed:28265003). Binding of SOLRL1 secreted N-terminal ectodomain to IL6 may increase IL6 trans signaling (PubMed:28265003). Interacts with secreted IL6R; this interaction leads to IL6R internalization (PubMed:28265003). Also interacts with transmembrane IL6R; this interaction does not affect IL6R subcellular location (PubMed:28265003). Interacts with APOE (PubMed:30448281). Interacts with apolipoprotein E-rich beta-VLDL (By similarity). Interacts with APOA5; this interaction leads to APOA5 internalization and is abolished by heparin (PubMed:17326667, PubMed:18603531). Interaction with APOA5 results in enhanced binding to chylomicrons (PubMed:17326667). Interacts with ROCK2 (PubMed:21147781). Interacts (via cytosolic C-terminus) with PPP3CB/calcineurin A beta (By similarity). Interacts with NTRK2/TRKB; this interaction facilitates NTRK2 trafficking between synaptic plasma membranes, postsynaptic densities and cell soma, hence positively regulates BDNF signaling (By similarity). Interacts (via cytosolic C-terminus) with HSPA12A in an ADP-dependent manner; this interaction affects SORL1 internalization and subcellular localization (PubMed:30679749). Interacts (via N-terminal ectodomain) with ERBB2/HER2 (PubMed:31138794).Q92673P05067false5Q92673P05067-4false8Q92673PRO_0000000091false4Q92673PRO_0000000093false3Q92673P83916false3Q92673P43681false3Q92673P26992false7Q92673O75462false3Q92673Q96D03false3Q92673P20042false3Q92673PRO_0000034005false6Q92673P56159-2false3Q92673Q9UJY5false4Q92673Q9UJY4false5Q92673O43301false5Q92673P05231false4Q92673P08887false7Q92673Q92993false3Q92673P30533false4Q92673P19404false3Q92673P00491false3Q92673P78424false3Q92673Q15669false3Q92673PRO_0000033164false9Q92673Q8N0S8false3Q92673Q62997true5Golgi apparatus membraneSingle-pass type I membrane proteinGolgi apparatusTrans-Golgi network membraneSingle-pass type I membrane proteinEndosome membraneSingle-pass type I membrane proteinEarly endosome membraneSingle-pass type I membrane proteinRecycling endosome membraneSingle-pass type I membrane proteinEndoplasmic reticulum membraneSingle-pass type I membrane proteinEndosomeMultivesicular body membraneSingle-pass type I membrane proteinCell membraneSingle-pass type I membrane proteinCytoplasmic vesicleSecretory vesicle membraneSingle-pass type I membrane proteinSecretedMostly intracellular, predominantly in the trans-Golgi network (TGN) and in endosome, as well as in endosome-to-TGN retrograde vesicles; found at low levels on the plasma membrane (PubMed:11294867, PubMed:15053742, PubMed:17855360, PubMed:21994944, PubMed:21385844, PubMed:31138794). At the cell surface, partially subjected to proteolytic shedding that releases the ectodomain (also called soluble SORLA, solLR11 or sLR11) in the extracellular milieu (PubMed:11082041, PubMed:16393139, PubMed:16531402). The shedding may be catalyzed by ADAM17/TACE (PubMed:16393139). Following shedding, PSEN1/presenilin-1 cleaves the remaining transmembrane fragment and catalyzes the release of a C-terminal fragment in the cytosol and of a soluble N-terminal beta fragment in the extracellular milieu. The C-terminal cytosolic fragment localizes to the nucleus (PubMed:16531402). At the cell surface, the full-length protein undergoes partial clathrin-dependent endocytosis guided by clathrin adapter protein 2 (AP-2) (PubMed:11294867, PubMed:15053742, PubMed:17646382).Highly expressed in brain (at protein level) (PubMed:9157966, PubMed:16174740, PubMed:21147781). Most abundant in the cerebellum, cerebral cortex and occipital pole; low levels in the putamen and thalamus (PubMed:9157966, PubMed:16174740). Expression is significantly reduced in the frontal cortex of patients suffering from Alzheimer disease (PubMed:16174740). Also expressed in spinal cord, spleen, testis, prostate, ovary, thyroid and lymph nodes (PubMed:9157966, PubMed:8940146).Up-regulated by morphogenetic neuropeptide, also called head activator or HA (PubMed:11082041). Up-regulated under hypoxic conditions in hematopoietic stem and progenitor cells, a physiological condition encountered by these cells in the endosteum. This up-regulation may be mediated by HIF1A-induced transcription (PubMed:23486467).Within the Golgi apparatus, the propeptide may be cleaved off by FURIN or a furin-like protease (Probable). After cleavage, the propeptide interacts with the mature protein N-terminus, preventing the association with other ligands (PubMed:11294867). At the cell surface, partially subjected to proteolytic shedding that releases the ectodomain in the extracellular milieu (PubMed:11082041, PubMed:16393139, PubMed:16531402, PubMed:28265003). The shedding may be catalyzed by ADAM17/TACE (PubMed:16393139, PubMed:16531402). Following shedding, PSEN1/presenilin-1 cleaves the remaining transmembrane fragment and catalyzes the release of a C-terminal fragment in the cytosol and of a soluble N-terminal beta fragment in the extracellular milieu. The C-terminal cytosolic fragment localizes to the nucleus (PubMed:16531402).Phosphorylation at Ser-2206 facilitates the interaction with GGA1.Alzheimer disease
AD
Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituents of these plaques are neurotoxic amyloid-beta protein 40 and amyloid-beta protein 42, that are produced by the proteolysis of the transmembrane APP protein. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products, such as C31, are also implicated in neuronal death.The gene represented in this entry may be involved in disease pathogenesis.There may be a positive correlation of body mass index with levels of SORL1 transcript and SORLA protein in visceral adipose tissue.Belongs to the VPS10-related sortilin family. SORL1 subfamily.3D-structureAlzheimer diseaseAmyloidosisCell membraneCleavage on pair of basic residuesCytoplasmic vesicleDirect protein sequencingDisease variantDisulfide bondEGF-like domainEndocytosisEndoplasmic reticulumEndosomeGlycoproteinGolgi apparatusMembraneNeurodegenerationPhosphoproteinReceptorReference proteomeRepeatSecretedSignalTransmembraneTransmembrane helixTransportLSYCGRATNSQENSMLGDVILVRRKRGRKGRRAAFANSHYAAASHADDLGEDDEDAALGAAAAADDAAEDDEDAAAAAMIAATGAAFSAADDAADVPMAVPAVPAAMATRSSRRESRLPFLFTLVALLPPGALCEVWTQRLHGGSAPLPQDRGFLVVQGDPRELRLWARGDARGASRADEKPLRRKRSAALQPEPIKVYGQVSLNDSHNQMVVHWAGEKSNVIVALARDSLALARPKSSDVYVSYDYGKSFKKISDKLNFGLGNRSEAVIAQFYHSPADNKRYIFADAYAQYLWITFDFCNTLQGFSIPFRAADLLLHSKASNLLLGFDRSHPNKQLWKSDDFGQTWIMIQEHVKSFSWGIDPYDKPNTIYIERHEPSGYSTVFRSTDFFQSRENQEVILEEVRDFQLRDKYMFATKVVHLLGSEQQSSVQLWVSFGRKPMRAAQFVTRHPINEYYIADASEDQVFVCVSHSNNRTNLYISEAEGLKFSLSLENVLYYSPGGAGSDTLVRYFANEPFADFHRVEGLQGVYIATLINGSMNEENMRSVITFDKGGTWEFLQAPAFTGYGEKINCELSQGCSLHLAQRLSQLLNLQLRRMPILSKESAPGLIIATGSVGKNLASKTNVYISSSAGARWREALPGPHYYTWGDHGGIITAIAQGMETNELKYSTNEGETWKTFIFSEKPVFVYGLLTEPGEKSTVFTIFGSNKENVHSWLILQVNATDALGVPCTENDYKLWSPSDERGNECLLGHKTVFKRRTPHATCFNGEDFDRPVVVSNCSCTREDYECDFGFKMSEDLSLEVCVPDPEFSGKSYSPPVPCPVGSTYRRTRGYRKISGDTCSGGDVEARLEGELVPCPLAEENEFILYAVRKSIYRYDLASGATEQLPLTGLRAAVALDFDYEHNCLYWSDLALDVIQRLCLNGSTGQEVIINSGLETVEALAFEPLSQLLYWVDAGFKKIEVANPDGDFRLTIVNSSVLDRPRALVLVPQEGVMFWTDWGDLKPGIYRSNMDGSAAYHLVSEDVKWPNGISVDDQWIYWTDAYLECIERITFSGQQRSVILDNLPHPYAIAVFKNEIYWDDWSQLSIFRASKYSGSQMEILANQLTGLMDMKIFYKGKNTGSNACVPRPCSLLCLPKANNSRSCRCPEDVSSSVLPSGDLMCDCPQGYQLKNNTCVKQENTCLRNQYRCSNGNCINSIWWCDFDNDCGDMSDERNCPTTICDLDTQFRCQESGTCIPLSYKCDLEDDCGDNSDESHCEMHQCRSDEYNCSSGMCIRSSWVCDGDNDCRDWSDEANCTAIYHTCEASNFQCRNGHCIPQRWACDGDTDCQDGSDEDPVNCEKKCNGFRCPNGTCIPSSKHCDGLRDCSDGSDEQHCEPLCTHFMDFVCKNRQQCLFHSMVCDGIIQCRDGSDEDAAFAGCSQDPEFHKVCDEFGFQCQNGVCISLIWKCDGMDDCGDYSDEANCENPTEAPNCSRYFQFRCENGHCIPNRWKCDRENDCGDWSDEKDCGDSHILPFSTPGPSTCLPNYYRCSSGTCVMDTWVCDGYRDCADGSDEEACPLLANVTAASTPTQLGRCDRFEFECHQPKTCIPNWKRCDGHQDCQDGRDEANCPTHSTLTCMSREFQCEDGEACIVLSERCDGFLDCSDESDEKACSDELTVYKVQNLQWTADFSGDVTLTWMRPKKMPSASCVYNVYYRVVGESIWKTLETHSNKTNTVLKVLKPDTTYQVKVQVQCLSKAHNTNDFVTLRTPEGLPDAPRNLQLSLPREAEGVIVGHWAPPIHTHGLIREYIVEYSRSGSKMWASQRAASNFTEIKNLLVNTLYTVRVAAVTSRGIGNWSDSKSITTIKGKVIPPPDIHIDSYGENYLSFTLTMESDIKVNGYVVNLFWAFDTHKQERRTLNFRGSILSHKVGNLTAHTSYEISAWAKTDLGDSPLAFEHVMTRGVRPPAPSLKAKAINQTAVECTWTGPRNVVYGIFYATSFLDLYRNPKSLTTSLHNKTVIVSKDEQYLFLVRVVVPYQGPSSDYVVVKMIPDSRLPPRHLHVVHTGKTSVVIKWESPYDSPDQDLLYAVAVKDLIRKTDRSYKVKSRNSTVEYTLNKLEPGGKYHIIVQLGNMSKDSSIKITTVSLSAPDALKIITENDHVLLFWKSLALKEKHFNESRGYEIHMFDSAMNITAYLGNTTDNFFKISNLKMGHNYTFTVQARCLFGNQICGEPAILLYDELGSGADASATQAARSTDVAAVVVPILFLILLSLGVGFAILYTKHRRLQSSFTAFANSHYSSRLGSAIFSSGDDLGEDDEDAPMITGFSDDVPMVIA
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