LRP5_MOUSE
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 03-AUG-2022, entry version 170.
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},
GN Lrp7 {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}.
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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 GlyGen; Q91VN0; 6 sites.
DR iPTMnet; Q91VN0; -.
DR PhosphoSitePlus; Q91VN0; -.
DR EPD; Q91VN0; -.
DR MaxQB; Q91VN0; -.
DR PaxDb; Q91VN0; -.
DR PRIDE; Q91VN0; -.
DR ProteomicsDB; 287274; -. [Q91VN0-1]
DR Antibodypedia; 4572; 407 antibodies from 37 providers.
DR DNASU; 16973; -.
DR Ensembl; ENSMUST00000025856; ENSMUSP00000025856; ENSMUSG00000024913. [Q91VN0-1]
DR GeneID; 16973; -.
DR KEGG; mmu:16973; -.
DR UCSC; uc008fwq.2; mouse. [Q91VN0-1]
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; DMEEFSA; -.
DR OrthoDB; 121310at2759; -.
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 75 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 164 other tissues.
DR ExpressionAtlas; Q91VN0; baseline and differential.
DR Genevisible; Q91VN0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0071936; F:coreceptor activity involved in Wnt signaling pathway; 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; ISO: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:0060348; P:bone development; IMP:BHF-UCL.
DR GO; GO:0048539; P:bone marrow development; ISO:MGI.
DR GO; GO:0060349; P:bone morphogenesis; ISO:MGI.
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:0060764; P:cell-cell signaling involved in mammary gland development; IMP:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
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:0035426; P:extracellular matrix-cell signaling; IDA:BHF-UCL.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IGI:MGI.
DR GO; GO:0006007; P:glucose catabolic process; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:MGI.
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:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISO:MGI.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:MGI.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; ISO: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 CDD; cd00112; LDLa; 3.
DR Gene3D; 2.120.10.30; -; 4.
DR Gene3D; 4.10.400.10; -; 3.
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 Pfam; PF00057; Ldl_recept_a; 3.
DR Pfam; PF00058; Ldl_recept_b; 14.
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; SSF57424; SSF57424; 3.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS51120; LDLRB; 20.
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
