ID LRP5_MOUSE Reviewed; 1614 AA. AC Q91VN0; E9QQ75; O88883; Q9R208; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 27-MAR-2024, entry version 179. DE RecName: Full=Low-density lipoprotein receptor-related protein 5 {ECO:0000303|PubMed:11956231}; DE Short=LRP-5; DE AltName: Full=Low-density lipoprotein receptor-related protein 7 {ECO:0000303|PubMed:10049586}; DE Short=LRP-7; DE Flags: Precursor; GN Name=Lrp5 {ECO:0000303|PubMed:11956231, ECO:0000312|MGI:MGI:1278315}; GN Synonyms=Lr3 {ECO:0000303|PubMed:10049586}, Lrp7 GN {ECO:0000303|PubMed:10049586}; 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] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=9714764; DOI=10.1016/s0378-1119(98)00311-4; RA Hey P.J., Twells R.C.J., Phillips M.S., Nakagawa Y., Brown S.D., RA Kawaguchi Y., Cox R., Xie G., Dugan V., Hammond H., Metzker M.L., RA Todd J.A., Hess J.F.; RT "Cloning of a novel member of the low-density lipoprotein receptor RT family."; RL Gene 216:103-111(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND TISSUE RP SPECIFICITY. RC TISSUE=Liver; RX PubMed=10049586; DOI=10.1006/geno.1998.5688; RA Chen D., Lathrop W., Dong Y.; RT "Molecular cloning of mouse Lrp7(Lr3) cDNA and chromosomal mapping of RT orthologous genes in mouse and human."; RL Genomics 55:314-321(1999). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP DEVELOPMENTAL STAGE. RX PubMed=11719191; DOI=10.1016/s0092-8674(01)00571-2; RA Gong Y., Slee R.B., Fukai N., Rawadi G., Roman-Roman S., Reginato A.M., RA Wang H., Cundy T., Glorieux F.H., Lev D., Zacharin M., Oexle K., RA Marcelino J., Suwairi W., Heeger S., Sabatakos G., Apte S., Adkins W.N., RA Allgrove J., Arslan-Kirchner M., Batch J.A., Beighton P., Black G.C., RA Boles R.G., Boon L.M., Borrone C., Brunner H.G., Carle G.F., RA Dallapiccola B., De Paepe A., Floege B., Halfhide M.L., Hall B., RA Hennekam R.C.M., Hirose T., Jans A., Jueppner H., Kim C.A., RA Keppler-Noreuil K., Kohlschuetter A., LaCombe D., Lambert M., Lemyre E., RA Letteboer T., Peltonen L., Ramesar R.S., Romanengo M., Somer H., RA Steichen-Gersdorf E., Steinmann B., Sullivan B., Superti-Furga A., RA Swoboda W., van den Boogaard M.-J., Van Hul W., Vikkula M., Votruba M., RA Zabel B., Garcia T., Baron R., Olsen B.R., Warman M.L.; RT "LDL receptor-related protein 5 (LRP5) affects bone accrual and eye RT development."; RL Cell 107:513-523(2001). RN [6] RP INTERACTION WITH MESD, OLIGOMERIZATION, AND SUBCELLULAR LOCATION. RX PubMed=12581525; DOI=10.1016/s0092-8674(03)00045-x; RA Hsieh J.-C., Lee L., Zhang L., Wefer S., Brown K., DeRossi C., Wines M.E., RA Rosenquist T., Holdener B.C.; RT "Mesd encodes an LRP5/6 chaperone essential for specification of mouse RT embryonic polarity."; RL Cell 112:355-367(2003). RN [7] RP DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=15142971; DOI=10.1242/dev.01137; RA Kelly O.G., Pinson K.I., Skarnes W.C.; RT "The Wnt co-receptors Lrp5 and Lrp6 are essential for gastrulation in RT mice."; RL Development 131:2803-2815(2004). RN [8] RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=11956231; DOI=10.1083/jcb.200201089; RA Kato M., Patel M.S., Levasseur R., Lobov I., Chang B.H., Glass D.A. II, RA Hartmann C., Li L., Hwang T.H., Brayton C.F., Lang R.A., Karsenty G., RA Chan L.; RT "Cbfa1-independent decrease in osteoblast proliferation, osteopenia, and RT persistent embryonic eye vascularization in mice deficient in Lrp5, a Wnt RT coreceptor."; RL J. Cell Biol. 157:303-314(2002). CC -!- FUNCTION: Acts as a coreceptor with members of the frizzled family of CC seven-transmembrane spanning receptors to transduce signal by Wnt CC proteins. Activates the canonical Wnt signaling pathway that controls CC cell fate determination and self-renewal during embryonic development CC and adult tissue regeneration (PubMed:11956231). In particular, may CC play an important role in the development of the posterior patterning CC of the epiblast during gastrulation (PubMed:15142971). During bone CC development, regulates osteoblast proliferation and differentiation CC thus determining bone mass (PubMed:11956231). Mechanistically, the CC formation of the signaling complex between Wnt ligand, frizzled CC receptor and LRP5 coreceptor promotes the recruitment of AXIN1 to LRP5, CC stabilizing beta-catenin/CTNNB1 and activating TCF/LEF-mediated CC transcriptional programs (By similarity). Acts as a coreceptor for non- CC Wnt proteins, such as norrin/NDP. Binding of norrin/NDP to frizzled CC 4/FZD4-LRP5 receptor complex triggers beta-catenin/CTNNB1-dependent CC signaling known to be required for retinal vascular development (By CC similarity). Plays a role in controlling postnatal vascular regression CC in retina via macrophage-induced endothelial cell apoptosis CC (PubMed:11956231). {ECO:0000250|UniProtKB:O75197, CC ECO:0000269|PubMed:11956231, ECO:0000269|PubMed:15142971}. CC -!- SUBUNIT: Homodimer; disulfide-linked. Forms phosphorylated oligomer CC aggregates on Wnt-signaling (PubMed:12581525). Component of a WNT- CC signaling complex that contains a WNT protein, a FZD protein and LRP5 CC or LRP6. Interacts with FZD8; the interaction is formed on WNT-binding CC and signaling. Interacts (via the phosphorylated PPPSP motif domains) CC with AXIN1; the interaction prevents inhibition of beta-catenin CC phosphorylation and signaling and is enhanced in the presence of GSK3B CC and WNT1 or WNT3A. Interacts (via beta-propeller regions 3 and 4) with CC DKK1; the interaction, enhanced by MESD and/or KREMEN, inhibits beta- CC catenin signaling by preventing GSK3-mediated phosphorylation of the CC PPPSP motifs and subsequent, AXIN1 binding. Interacts with CSNK1E. CC Interacts with SOST; the interaction antagonizes canonical Wnt CC signaling. Interacts with APCDD1 (By similarity). Interacts with MESD; CC the interaction prevents the formation of LRP5 aggregates, targets LRP5 CC to the plasma membrane and, when complexed with KREMEN2, increases DKK1 CC binding (PubMed:12581525). Interacts with CAPRIN2 (By similarity). CC {ECO:0000250|UniProtKB:O75197, ECO:0000269|PubMed:12581525}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12581525}; Single- CC pass type I membrane protein {ECO:0000269|PubMed:12581525}. Endoplasmic CC reticulum {ECO:0000269|PubMed:12581525}. Note=Chaperoned to the plasma CC membrane by MESD. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced.; CC Name=1; CC IsoId=Q91VN0-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Widely expressed, with the highest expression CC levels in liver, heart, and lung and the lowest levels in brain and CC spleen. {ECO:0000269|PubMed:10049586, ECO:0000269|PubMed:11956231}. CC -!- DEVELOPMENTAL STAGE: Expressed in early embryo throughout the ectoderm CC at 6.5 dpc and in visceral endoderm overlying the extraembryonic CC ectoderm at 7.5 dpc. Not present in the mesoderm nor in endoderm CC emerging from the primitive streak (PubMed:15142971). Expressed in CC differentiating osteoblasts that contribute to the lateral membranous CC part of clavicle at embryonic day 13.5. Expressed in osteoblasts lining CC the bony trabeculae of the humerus at embryonic day 16.5. Expressed in CC osteoblasts on both surfaces of the temporal bone at embryonic day 17.5 CC (PubMed:11719191). {ECO:0000269|PubMed:11719191, CC ECO:0000269|PubMed:15142971}. CC -!- PTM: Phosphorylation of cytoplasmic PPPSP motifs regulates the signal CC transduction of the Wnt signaling pathway through acting as a docking CC site for AXIN1. {ECO:0000250|UniProtKB:O75197}. CC -!- DISRUPTION PHENOTYPE: Mice exhibit decreased osteoblast proliferation, CC developing low bone mass postnatally. Also display persistent embryonic CC eye vascularization due to a failure of macrophage-induced endothelial CC cell apoptosis. Mutant animals exhibit a loss of middle phalanx CC ossification at 18.5 dpc. LRP5 and LRP6 double null mutants are more CC severely affected. Embryos arrest prior to mid-gestation. CC {ECO:0000269|PubMed:11956231, ECO:0000269|PubMed:15142971}. CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}. 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; AF064984; AAC36468.1; -; mRNA. DR EMBL; AF077847; AAC70183.1; -; mRNA. DR EMBL; AC112990; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC117797; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC011374; AAH11374.1; -; mRNA. DR CCDS; CCDS37881.1; -. [Q91VN0-1] DR RefSeq; NP_032539.2; NM_008513.3. [Q91VN0-1] DR AlphaFoldDB; Q91VN0; -. DR SMR; Q91VN0; -. DR BioGRID; 201202; 12. DR CORUM; Q91VN0; -. DR IntAct; Q91VN0; 2. DR MINT; Q91VN0; -. DR STRING; 10090.ENSMUSP00000025856; -. DR ChEMBL; CHEMBL4296099; -. DR GlyCosmos; Q91VN0; 6 sites, No reported glycans. DR GlyGen; Q91VN0; 7 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q91VN0; -. DR PhosphoSitePlus; Q91VN0; -. DR EPD; Q91VN0; -. DR MaxQB; Q91VN0; -. DR PaxDb; 10090-ENSMUSP00000025856; -. DR ProteomicsDB; 287274; -. [Q91VN0-1] DR Pumba; Q91VN0; -. DR Antibodypedia; 4572; 486 antibodies from 37 providers. DR DNASU; 16973; -. DR Ensembl; ENSMUST00000025856.17; ENSMUSP00000025856.11; ENSMUSG00000024913.17. [Q91VN0-1] DR GeneID; 16973; -. DR KEGG; mmu:16973; -. DR UCSC; uc008fwq.2; mouse. [Q91VN0-1] DR AGR; MGI:1278315; -. DR CTD; 4041; -. DR MGI; MGI:1278315; Lrp5. DR VEuPathDB; HostDB:ENSMUSG00000024913; -. DR eggNOG; KOG1215; Eukaryota. DR GeneTree; ENSGT00940000156574; -. DR HOGENOM; CLU_002489_0_0_1; -. DR InParanoid; Q91VN0; -. DR OMA; HTPCEDN; -. DR OrthoDB; 3107655at2759; -. DR PhylomeDB; Q91VN0; -. DR TreeFam; TF315253; -. DR Reactome; R-MMU-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists. DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane. DR Reactome; R-MMU-4641263; Regulation of FZD by ubiquitination. DR BioGRID-ORCS; 16973; 2 hits in 80 CRISPR screens. DR ChiTaRS; Lrp5; mouse. DR PRO; PR:Q91VN0; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; Q91VN0; Protein. DR Bgee; ENSMUSG00000024913; Expressed in epithelium of urethra and 166 other cell types or tissues. DR ExpressionAtlas; Q91VN0; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0043235; C:receptor complex; ISO:MGI. DR GO; GO:0015026; F:coreceptor activity; ISO:MGI. DR GO; GO:0042813; F:Wnt receptor activity; IDA:MGI. DR GO; GO:0017147; F:Wnt-protein binding; IPI:MGI. DR GO; GO:0060612; P:adipose tissue development; IBA:GO_Central. DR GO; GO:0006865; P:amino acid transport; IMP:MGI. DR GO; GO:0060033; P:anatomical structure regression; IMP:MGI. DR GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI. DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IMP:MGI. DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI. DR GO; GO:0060348; P:bone development; IMP:BHF-UCL. DR GO; GO:0048539; P:bone marrow development; IBA:GO_Central. DR GO; GO:0060349; P:bone morphogenesis; IBA:GO_Central. DR GO; GO:0046849; P:bone remodeling; IMP:MGI. DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI. DR GO; GO:0042074; P:cell migration involved in gastrulation; IGI:MGI. DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI. DR GO; GO:0060764; P:cell-cell signaling involved in mammary gland development; IMP:MGI. DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central. DR GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI. DR GO; GO:0042733; P:embryonic digit morphogenesis; IGI:MGI. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0060856; P:establishment of blood-brain barrier; IMP:MGI. DR GO; GO:1990963; P:establishment of blood-retinal barrier; IMP:MGI. DR GO; GO:0035426; P:extracellular matrix-cell signaling; IDA:BHF-UCL. DR GO; GO:0001702; P:gastrulation with mouth forming second; IGI:MGI. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0006007; P:glucose catabolic process; IEA:Ensembl. DR GO; GO:0035108; P:limb morphogenesis; IGI:MGI. DR GO; GO:0060603; P:mammary gland duct morphogenesis; IGI:MGI. DR GO; GO:0008078; P:mesodermal cell migration; IGI:MGI. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl. DR GO; GO:0110135; P:Norrin signaling pathway; IDA:BHF-UCL. DR GO; GO:0002076; P:osteoblast development; IMP:BHF-UCL. DR GO; GO:0033687; P:osteoblast proliferation; IMP:MGI. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl. DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl. DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL. DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI. DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl. DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI. DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl. DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl. DR GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:MGI. DR GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; IMP:MGI. DR GO; GO:0061304; P:retinal blood vessel morphogenesis; IMP:CACAO. DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI. DR GO; GO:0001944; P:vasculature development; IMP:MGI. DR GO; GO:0016055; P:Wnt signaling pathway; IMP:MGI. DR CDD; cd00112; LDLa; 3. DR Gene3D; 2.10.25.10; Laminin; 1. DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3. DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 4. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR036055; LDL_receptor-like_sf. DR InterPro; IPR023415; LDLR_class-A_CS. DR InterPro; IPR000033; LDLR_classB_rpt. DR InterPro; IPR002172; LDrepeatLR_classA_rpt. DR InterPro; IPR017049; LRP5/6. DR PANTHER; PTHR46513:SF16; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 5; 1. DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1. DR Pfam; PF14670; FXa_inhibition; 3. DR Pfam; PF00057; Ldl_recept_a; 3. DR Pfam; PF00058; Ldl_recept_b; 13. DR PIRSF; PIRSF036314; LDL_recpt-rel_p5/6; 1. DR PRINTS; PR00261; LDLRECEPTOR. DR SMART; SM00181; EGF; 4. DR SMART; SM00192; LDLa; 3. DR SMART; SM00135; LY; 20. DR SUPFAM; SSF57196; EGF/Laminin; 4. DR SUPFAM; SSF57424; LDL receptor-like module; 3. DR SUPFAM; SSF63825; YWTD domain; 4. DR PROSITE; PS01209; LDLRA_1; 3. DR PROSITE; PS50068; LDLRA_2; 3. DR PROSITE; PS51120; LDLRB; 20. DR Genevisible; Q91VN0; MM. PE 1: Evidence at protein level; KW Alternative splicing; Developmental protein; Disulfide bond; KW EGF-like domain; Endocytosis; Endoplasmic reticulum; Glycoprotein; KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix; Wnt signaling pathway. FT SIGNAL 1..30 FT /evidence="ECO:0000255" FT CHAIN 31..1614 FT /note="Low-density lipoprotein receptor-related protein 5" FT /id="PRO_0000017329" FT TOPO_DOM 31..1383 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1384..1406 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1407..1614 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 74..118 FT /note="LDL-receptor class B 1" FT REPEAT 119..161 FT /note="LDL-receptor class B 2" FT REPEAT 162..205 FT /note="LDL-receptor class B 3" FT REPEAT 206..246 FT /note="LDL-receptor class B 4" FT REPEAT 247..289 FT /note="LDL-receptor class B 5" FT DOMAIN 294..336 FT /note="EGF-like 1" FT REPEAT 384..426 FT /note="LDL-receptor class B 6" FT REPEAT 427..469 FT /note="LDL-receptor class B 7" FT REPEAT 470..513 FT /note="LDL-receptor class B 8" FT REPEAT 514..556 FT /note="LDL-receptor class B 9" FT REPEAT 557..599 FT /note="LDL-receptor class B 10" FT DOMAIN 600..640 FT /note="EGF-like 2" FT REPEAT 686..728 FT /note="LDL-receptor class B 11" FT REPEAT 729..771 FT /note="LDL-receptor class B 12" FT REPEAT 772..814 FT /note="LDL-receptor class B 13" FT REPEAT 815..854 FT /note="LDL-receptor class B 14" FT REPEAT 855..897 FT /note="LDL-receptor class B 15" FT DOMAIN 901..941 FT /note="EGF-like 3" FT REPEAT 988..1034 FT /note="LDL-receptor class B 16" FT REPEAT 1035..1077 FT /note="LDL-receptor class B 17" FT REPEAT 1078..1122 FT /note="LDL-receptor class B 18" FT REPEAT 1123..1164 FT /note="LDL-receptor class B 19" FT REPEAT 1165..1206 FT /note="LDL-receptor class B 20" FT DOMAIN 1212..1253 FT /note="EGF-like 4" FT DOMAIN 1257..1295 FT /note="LDL-receptor class A 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 1296..1332 FT /note="LDL-receptor class A 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 1334..1370 FT /note="LDL-receptor class A 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT REGION 31..287 FT /note="Beta-propeller 1" FT REGION 340..601 FT /note="Beta-propeller 2" FT REGION 643..902 FT /note="Beta-propeller 3" FT REGION 944..1211 FT /note="Beta-propeller 4" FT REGION 1002..1025 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1474..1498 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1567..1599 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1499..1505 FT /note="PPPSP motif A" FT MOTIF 1537..1544 FT /note="PPPSP motif B" FT MOTIF 1573..1580 FT /note="PPPSP motif C" FT MOTIF 1590..1595 FT /note="PPPSP motif D" FT MOTIF 1604..1611 FT /note="PPPSP motif E" FT COMPBIAS 1007..1024 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1475..1493 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 92 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 137 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 445 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 498 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 704 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 877 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 298..309 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 305..320 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 322..335 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 604..615 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 611..624 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 626..639 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 905..916 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 912..925 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 927..940 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1216..1227 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1223..1237 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1239..1252 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1258..1272 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1265..1285 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1279..1294 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1297..1309 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1304..1322 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1316..1331 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1335..1347 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1342..1360 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DISULFID 1354..1369 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT CONFLICT 220 FT /note="R -> H (in Ref. 2; AAC70183)" FT /evidence="ECO:0000305" FT CONFLICT 1520 FT /note="I -> S (in Ref. 4; AAH11374)" FT /evidence="ECO:0000305" FT CONFLICT 1553 FT /note="T -> I (in Ref. 1; AAC36468 and 2; AAC70183)" FT /evidence="ECO:0000305" SQ SEQUENCE 1614 AA; 178885 MW; 80FF4288470A4FC5 CRC64; METAPTRAPP PPPPPLLLLV LYCSLVPAAA SPLLLFANRR DVRLVDAGGV KLESTIVASG LEDAAAVDFQ FSKGAVYWTD VSEEAIKQTY LNQTGAAAQN IVISGLVSPD GLACDWVGKK LYWTDSETNR IEVANLNGTS RKVLFWQDLD QPRAIALDPA HGYMYWTDWG EAPRIERAGM DGSTRKIIVD SDIYWPNGLT IDLEEQKLYW ADAKLSFIHR ANLDGSFRQK VVEGSLTHPF ALTLSGDTLY WTDWQTRSIH ACNKWTGEQR KEILSALYSP MDIQVLSQER QPPFHTPCEE DNGGCSHLCL LSPREPFYSC ACPTGVQLQD NGKTCKTGAE EVLLLARRTD LRRISLDTPD FTDIVLQVGD IRHAIAIDYD PLEGYVYWTD DEVRAIRRAY LDGSGAQTLV NTEINDPDGI AVDWVARNLY WTDTGTDRIE VTRLNGTSRK ILVSEDLDEP RAIVLHPVMG LMYWTDWGEN PKIECANLDG RDRHVLVNTS LGWPNGLALD LQEGKLYWGD AKTDKIEVIN IDGTKRKTLL EDKLPHIFGF TLLGDFIYWT DWQRRSIERV HKVKASRDVI IDQLPDLMGL KAVNVAKVVG TNPCADGNGG CSHLCFFTPR ATKCGCPIGL ELLSDMKTCI IPEAFLVFTS RATIHRISLE TNNNDVAIPL TGVKEASALD FDVSNNHIYW TDVSLKTISR AFMNGSSVEH VIEFGLDYPE GMAVDWMGKN LYWADTGTNR IEVARLDGQF RQVLVWRDLD NPRSLALDPT KGYIYWTEWG GKPRIVRAFM DGTNCMTLVD KVGRANDLTI DYADQRLYWT DLDTNMIESS NMLGQERMVI ADDLPYPFGL TQYSDYIYWT DWNLHSIERA DKTSGRNRTL IQGHLDFVMD ILVFHSSRQD GLNDCVHSNG QCGQLCLAIP GGHRCGCASH YTLDPSSRNC SPPSTFLLFS QKFAISRMIP DDQLSPDLVL PLHGLRNVKA INYDPLDKFI YWVDGRQNIK RAKDDGTQPS MLTSPSQSLS PDRQPHDLSI DIYSRTLFWT CEATNTINVH RLDGDAMGVV LRGDRDKPRA IAVNAERGYM YFTNMQDHAA KIERASLDGT EREVLFTTGL IRPVALVVDN ALGKLFWVDA DLKRIESCDL SGANRLTLED ANIVQPVGLT VLGRHLYWID RQQQMIERVE KTTGDKRTRV QGRVTHLTGI HAVEEVSLEE FSAHPCARDN GGCSHICIAK GDGTPRCSCP VHLVLLQNLL TCGEPPTCSP DQFACTTGEI DCIPGAWRCD GFPECADQSD EEGCPVCSAS QFPCARGQCV DLRLRCDGEA DCQDRSDEAN CDAVCLPNQF RCTSGQCVLI KQQCDSFPDC ADGSDELMCE INKPPSDDIP AHSSAIGPVI GIILSLFVMG GVYFVCQRVM CQRYTGASGP FPHEYVGGAP HVPLNFIAPG GSQHGPFPGI PCSKSVMSSM SLVGGRGSVP LYDRNHVTGA SSSSSSSTKA TLYPPILNPP PSPATDPSLY NVDVFYSSGI PATARPYRPY VIRGMAPPTT PCSTDVCDSD YSTSRWKSSK YYLDLNSDSD PYPPPPTPHS QYLSAEDSCP PSPGTERSYC HLFPPPPSPC TDSS //