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Low-density lipoprotein receptor-related protein 4 (LRP-4) (Multiple epidermal growth factor-like domains 7)

 LRP4_HUMAN              Reviewed;        1905 AA.
O75096; B2RN39; Q4AC85; Q5KTZ5;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 4.
22-NOV-2017, entry version 157.
RecName: Full=Low-density lipoprotein receptor-related protein 4;
Short=LRP-4;
AltName: Full=Multiple epidermal growth factor-like domains 7;
Flags: Precursor;
Name=LRP4; Synonyms=KIAA0816, LRP10, MEGF7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-1086; GLY-1554 AND
GLN-1646.
TISSUE=Brain;
Ishikawa K., Fujimoto H., Kim D., Saeki S.;
"Low density lipoprotein receptor-related protein 10.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-1086;
GLY-1554 AND GLN-1646.
TISSUE=Brain;
PubMed=9693030; DOI=10.1006/geno.1998.5341;
Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
"Identification of high-molecular-weight proteins with multiple EGF-
like motifs by motif-trap screening.";
Genomics 51:27-34(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-1086;
GLY-1554 AND GLN-1646.
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION IN THE REGULATION OF CANONICAL WTN SIGNALING, VARIANTS CLSS
ASN-137; TYR-160; ASN-449; PRO-461; PHE-473; ASN-529 AND ARG-1017, AND
CHARACTERIZATION OF VARIANTS CLSS ASN-137; TYR-160; ASN-449; PHE-473
AND ASN-529.
PubMed=20381006; DOI=10.1016/j.ajhg.2010.03.004;
Li Y., Pawlik B., Elcioglu N., Aglan M., Kayserili H., Yigit G.,
Percin F., Goodman F., Nurnberg G., Cenani A., Urquhart J.,
Chung B.D., Ismail S., Amr K., Aslanger A.D., Becker C., Netzer C.,
Scambler P., Eyaid W., Hamamy H., Clayton-Smith J., Hennekam R.,
Nurnberg P., Herz J., Temtamy S.A., Wollnik B.;
"LRP4 mutations alter Wnt/beta-catenin signaling and cause limb and
kidney malformations in Cenani-Lenz syndrome.";
Am. J. Hum. Genet. 86:696-706(2010).
[6]
FUNCTION, INTERACTION WITH SOST, TISSUE SPECIFICITY, VARIANTS SOST2
TRP-1170 AND SER-1186, CHARACTERIZATION OF VARIANTS SOST2 TRP-1170 AND
SER-1186, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=21471202; DOI=10.1074/jbc.M110.190330;
Leupin O., Piters E., Halleux C., Hu S., Kramer I., Morvan F.,
Bouwmeester T., Schirle M., Bueno-Lozano M., Fuentes F.J., Itin P.H.,
Boudin E., de Freitas F., Jennes K., Brannetti B., Charara N.,
Ebersbach H., Geisse S., Lu C.X., Bauer A., Van Hul W., Kneissel M.;
"Bone overgrowth-associated mutations in the LRP4 gene impair
sclerostin facilitator function.";
J. Biol. Chem. 286:19489-19500(2011).
[7]
INVOLVEMENT IN CMS17, VARIANTS SOST2 TRP-1170 AND SER-1186, VARIANTS
CMS17 LYS-1233 AND HIS-1277, CHARACTERIZATION OF VARIANTS SOST2
TRP-1170 AND SER-1186, CHARACTERIZATION OF VARIANTS CMS17 LYS-1233 AND
HIS-1277, AND MUTAGENESIS OF ASN-1214; VAL-1252; TYR-1256 AND
ILE-1287.
PubMed=24234652; DOI=10.1093/hmg/ddt578;
Ohkawara B., Cabrera-Serrano M., Nakata T., Milone M., Asai N.,
Ito K., Ito M., Masuda A., Ito Y., Engel A.G., Ohno K.;
"LRP4 third beta-propeller domain mutations cause novel congenital
myasthenia by compromising agrin-mediated MuSK signaling in a
position-specific manner.";
Hum. Mol. Genet. 23:1856-1868(2014).
-!- FUNCTION: Mediates SOST-dependent inhibition of bone formation.
Functions as a specific facilitator of SOST-mediated inhibition of
Wnt signaling. Plays a key role in the formation and the
maintenance of the neuromuscular junction (NMJ), the synapse
between motor neuron and skeletal muscle. Directly binds AGRIN and
recruits it to the MUSK signaling complex. Mediates the AGRIN-
induced phosphorylation of MUSK, the kinase of the complex. The
activation of MUSK in myotubes induces the formation of NMJ by
regulating different processes including the transcription of
specific genes and the clustering of AChR in the postsynaptic
membrane. Alternatively, may be involved in the negative
regulation of the canonical Wnt signaling pathway, being able to
antagonize the LRP6-mediated activation of this pathway. More
generally, has been proposed to function as a cell surface
endocytic receptor binding and internalizing extracellular ligands
for degradation by lysosomes. May play an essential role in the
process of digit differentiation (By similarity).
{ECO:0000250|UniProtKB:Q8VI56, ECO:0000269|PubMed:20381006,
ECO:0000269|PubMed:21471202}.
-!- SUBUNIT: Homooligomer. Interacts with MUSK; the heterodimer forms
an AGRIN receptor complex that binds AGRIN resulting in activation
of MUSK (By similarity). Interacts (via the extracellular domain)
with SOST; the interaction facilitates the inhibition of Wnt
signaling (PubMed:21471202). Interacts with MESD; the interaction
promotes glycosylation of LRP4 and its cell-surface expression (By
similarity). {ECO:0000250|UniProtKB:Q8VI56,
ECO:0000269|PubMed:21471202}.
-!- INTERACTION:
Q9BQB4:SOST; NbExp=4; IntAct=EBI-310873, EBI-5746563;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q8VI56}; Single-pass type I membrane
protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Expressed in bone; present in osteoblasts and
osteocytes. No expression is observed in osteoclast. Expressed in
several regions of the brain. {ECO:0000269|PubMed:21471202}.
-!- DISEASE: Cenani-Lenz syndactyly syndrome (CLSS) [MIM:212780]: A
congenital malformation syndrome defined as complete and complex
syndactyly of the hands combined with malformations of the forearm
bones and similar manifestations in the lower limbs. It is
characterized by fusion and disorganization of metacarpal and
phalangeal bones, radius and ulnar shortening, radioulnar
synostosis, and severe syndactyly of hands and feet.
{ECO:0000269|PubMed:20381006}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Sclerosteosis 2 (SOST2) [MIM:614305]: A sclerosing bone
dysplasia characterized by a generalized hyperostosis and
sclerosis leading to a markedly thickened skull, with mandible,
ribs, clavicles and all long bones also being affected. Due to
narrowing of the foramina of the cranial nerves, facial nerve
palsy, hearing loss and atrophy of the optic nerves can occur.
Sclerosteosis is clinically and radiologically very similar to van
Buchem disease, mainly differentiated by hand malformations and a
large stature in sclerosteosis patients.
{ECO:0000269|PubMed:21471202, ECO:0000269|PubMed:24234652}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Myasthenic syndrome, congenital, 17 (CMS17) [MIM:616304]:
A form of congenital myasthenic syndrome, a group of disorders
characterized by failure of neuromuscular transmission, including
pre-synaptic, synaptic, and post-synaptic disorders that are not
of autoimmune origin. Clinical features are easy fatigability and
muscle weakness affecting the axial and limb muscles (with
hypotonia in early-onset forms), the ocular muscles (leading to
ptosis and ophthalmoplegia), and the facial and bulbar musculature
(affecting sucking and swallowing, and leading to dysphonia). The
symptoms fluctuate and worsen with physical effort.
{ECO:0000269|PubMed:24234652}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE19679.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB084910; BAD83615.1; -; mRNA.
EMBL; AB011540; BAA32468.1; -; mRNA.
EMBL; AB231861; BAE19679.1; ALT_INIT; mRNA.
EMBL; AC021573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC037360; AAH37360.1; -; mRNA.
EMBL; BC041048; AAH41048.1; -; mRNA.
EMBL; BC136667; AAI36668.1; -; mRNA.
EMBL; BC136668; AAI36669.1; -; mRNA.
CCDS; CCDS31478.1; -.
RefSeq; NP_002325.2; NM_002334.3.
UniGene; Hs.4930; -.
ProteinModelPortal; O75096; -.
SMR; O75096; -.
BioGrid; 110218; 33.
IntAct; O75096; 5.
STRING; 9606.ENSP00000367888; -.
iPTMnet; O75096; -.
PhosphoSitePlus; O75096; -.
BioMuta; LRP4; -.
EPD; O75096; -.
MaxQB; O75096; -.
PaxDb; O75096; -.
PeptideAtlas; O75096; -.
PRIDE; O75096; -.
TopDownProteomics; O75096; -.
Ensembl; ENST00000378623; ENSP00000367888; ENSG00000134569.
GeneID; 4038; -.
KEGG; hsa:4038; -.
UCSC; uc001ndn.5; human.
CTD; 4038; -.
DisGeNET; 4038; -.
EuPathDB; HostDB:ENSG00000134569.9; -.
GeneCards; LRP4; -.
H-InvDB; HIX0009607; -.
HGNC; HGNC:6696; LRP4.
HPA; HPA011934; -.
HPA; HPA012300; -.
MalaCards; LRP4; -.
MIM; 212780; phenotype.
MIM; 604270; gene.
MIM; 614305; phenotype.
MIM; 616304; phenotype.
neXtProt; NX_O75096; -.
OpenTargets; ENSG00000134569; -.
Orphanet; 3258; Cenani-Lenz syndrome.
Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
Orphanet; 3152; Sclerosteosis.
PharmGKB; PA30454; -.
eggNOG; KOG1215; Eukaryota.
eggNOG; ENOG410XPR2; LUCA.
GeneTree; ENSGT00760000118968; -.
HOGENOM; HOG000047507; -.
HOVERGEN; HBG049163; -.
InParanoid; O75096; -.
KO; K20051; -.
OMA; LNGSNME; -.
OrthoDB; EOG091G0178; -.
PhylomeDB; O75096; -.
TreeFam; TF315253; -.
Reactome; R-HSA-3000178; ECM proteoglycans.
SIGNOR; O75096; -.
ChiTaRS; LRP4; human.
GeneWiki; Low_density_lipoprotein_receptor-related_protein_4; -.
GenomeRNAi; 4038; -.
PRO; PR:O75096; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000134569; -.
CleanEx; HS_LRP4; -.
ExpressionAtlas; O75096; baseline and differential.
Genevisible; O75096; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0097060; C:synaptic membrane; ISS:UniProtKB.
GO; GO:0034185; F:apolipoprotein binding; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0030971; F:receptor tyrosine kinase binding; ISS:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; ISS:UniProtKB.
GO; GO:0042813; F:Wnt-activated receptor activity; IBA:GO_Central.
GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
GO; GO:0030509; P:BMP signaling pathway; IEA:InterPro.
GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
GO; GO:0001822; P:kidney development; IDA:UniProtKB.
GO; GO:0060173; P:limb development; IDA:UniProtKB.
GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0030279; P:negative regulation of ossification; IMP:UniProtKB.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:1901631; P:positive regulation of presynaptic membrane organization; ISS:UniProtKB.
GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
GO; GO:0097104; P:postsynaptic membrane assembly; ISS:UniProtKB.
GO; GO:0097105; P:presynaptic membrane assembly; ISS:UniProtKB.
GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
GO; GO:0050808; P:synapse organization; ISS:UniProtKB.
GO; GO:0051124; P:synaptic growth at neuromuscular junction; ISS:UniProtKB.
GO; GO:0044332; P:Wnt signaling pathway involved in dorsal/ventral axis specification; IBA:GO_Central.
CDD; cd00112; LDLa; 7.
Gene3D; 2.120.10.30; -; 4.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR026823; cEGF.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR030799; LRP4.
PANTHER; PTHR44017:SF4; PTHR44017:SF4; 1.
Pfam; PF12662; cEGF; 1.
Pfam; PF00057; Ldl_recept_a; 8.
Pfam; PF00058; Ldl_recept_b; 16.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 7.
SMART; SM00179; EGF_CA; 3.
SMART; SM00192; LDLa; 8.
SMART; SM00135; LY; 20.
SUPFAM; SSF57184; SSF57184; 2.
SUPFAM; SSF57424; SSF57424; 8.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS01209; LDLRA_1; 8.
PROSITE; PS50068; LDLRA_2; 8.
PROSITE; PS51120; LDLRB; 20.
1: Evidence at protein level;
Calcium; Cell membrane; Complete proteome;
Congenital myasthenic syndrome; Developmental protein;
Differentiation; Disease mutation; Disulfide bond; EGF-like domain;
Endocytosis; Glycoprotein; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Wnt signaling pathway.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 1905 Low-density lipoprotein receptor-related
protein 4.
/FTId=PRO_0000017325.
TOPO_DOM 21 1725 Extracellular. {ECO:0000255}.
TRANSMEM 1726 1746 Helical. {ECO:0000255}.
TOPO_DOM 1747 1905 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 67 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 70 106 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 109 144 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 147 183 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 190 226 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 230 266 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 269 305 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 311 350 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 354 394 EGF-like 1; calcium-binding.
{ECO:0000255}.
DOMAIN 395 434 EGF-like 2; calcium-binding.
{ECO:0000255}.
REPEAT 480 522 LDL-receptor class B 1.
REPEAT 523 565 LDL-receptor class B 2.
REPEAT 566 609 LDL-receptor class B 3.
REPEAT 610 652 LDL-receptor class B 4.
REPEAT 653 693 LDL-receptor class B 5.
DOMAIN 698 737 EGF-like 3.
REPEAT 785 827 LDL-receptor class B 6.
REPEAT 828 870 LDL-receptor class B 7.
REPEAT 871 914 LDL-receptor class B 8.
REPEAT 915 956 LDL-receptor class B 9.
REPEAT 957 998 LDL-receptor class B 10.
REPEAT 1093 1135 LDL-receptor class B 11.
REPEAT 1136 1178 LDL-receptor class B 12.
REPEAT 1179 1222 LDL-receptor class B 13.
REPEAT 1223 1263 LDL-receptor class B 14.
REPEAT 1264 1306 LDL-receptor class B 15.
REPEAT 1397 1439 LDL-receptor class B 16.
REPEAT 1440 1482 LDL-receptor class B 17.
REPEAT 1483 1526 LDL-receptor class B 18.
REPEAT 1527 1568 LDL-receptor class B 19.
REPEAT 1569 1610 LDL-receptor class B 20.
MOTIF 1766 1769 Endocytosis signal. {ECO:0000255}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 719 719 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 901 901 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1077 1077 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1415 1415 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1467 1467 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 44 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 34 57 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 51 66 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 71 83 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 78 96 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 90 105 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 110 122 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 117 135 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 129 143 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 148 160 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 155 173 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 167 182 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 191 203 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 198 216 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 210 225 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 231 243 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 238 256 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 250 265 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 270 282 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 277 295 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 289 304 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 312 324 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 319 337 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 331 349 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 358 369 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 365 378 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 380 393 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 399 409 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 405 418 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 420 433 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 702 713 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 709 722 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 724 736 {ECO:0000255|PROSITE-ProRule:PRU00124}.
VARIANT 137 137 D -> N (in CLSS; abolishes the
antagonistic effect of LRP4 on LRP6-
mediated activation of Wnt signaling;
dbSNP:rs267607222).
{ECO:0000269|PubMed:20381006}.
/FTId=VAR_063776.
VARIANT 160 160 C -> Y (in CLSS; abolishes the
antagonistic effect of LRP4 on LRP6-
mediated activation of Wnt signaling;
dbSNP:rs267607221).
{ECO:0000269|PubMed:20381006}.
/FTId=VAR_063777.
VARIANT 314 314 L -> S (in dbSNP:rs7926667).
/FTId=VAR_058290.
VARIANT 449 449 D -> N (in CLSS; abolishes the
antagonistic effect of LRP4 on LRP6-
mediated activation of Wnt signaling;
dbSNP:rs267607224).
{ECO:0000269|PubMed:20381006}.
/FTId=VAR_063778.
VARIANT 461 461 T -> P (in CLSS; dbSNP:rs267607223).
{ECO:0000269|PubMed:20381006}.
/FTId=VAR_063779.
VARIANT 473 473 L -> F (in CLSS; abolishes the
antagonistic effect of LRP4 on LRP6-
mediated activation of Wnt signaling).
{ECO:0000269|PubMed:20381006}.
/FTId=VAR_063780.
VARIANT 529 529 D -> N (in CLSS; abolishes the
antagonistic effect of LRP4 on LRP6-
mediated activation of Wnt signaling;
dbSNP:rs267607220).
{ECO:0000269|PubMed:20381006}.
/FTId=VAR_063781.
VARIANT 1017 1017 C -> R (in CLSS).
{ECO:0000269|PubMed:20381006}.
/FTId=VAR_063782.
VARIANT 1086 1086 I -> V (in dbSNP:rs6485702).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9693030,
ECO:0000269|Ref.1}.
/FTId=VAR_057955.
VARIANT 1170 1170 R -> W (in SOST2; impairs the interaction
with SOST; loss of function as
facilitator of SOST-mediated inhibition
of Wnt signaling; has no effect on AGRN-
mediated MUSK signaling; retains the
ability to bind AGRN and MUSK;
dbSNP:rs387906884).
{ECO:0000269|PubMed:21471202,
ECO:0000269|PubMed:24234652}.
/FTId=VAR_066630.
VARIANT 1186 1186 W -> S (in SOST2; impairs the interaction
with SOST; loss of function as
facilitator of SOST-mediated inhibition
of Wnt signaling; has no effect on AGRN-
mediated MUSK signaling; retains the
ability to bind AGRN and MUSK;
dbSNP:rs387906883).
{ECO:0000269|PubMed:21471202,
ECO:0000269|PubMed:24234652}.
/FTId=VAR_066631.
VARIANT 1203 1203 A -> V (in dbSNP:rs2306033).
/FTId=VAR_058291.
VARIANT 1233 1233 E -> K (in CMS17; decreases binding
affinity for AGRN and MUSK proteins; does
not enhance downstream activation of the
MUSK signaling pathway thus impairing
clustering of AChRs; dbSNP:rs786205153).
{ECO:0000269|PubMed:24234652}.
/FTId=VAR_073695.
VARIANT 1238 1238 A -> T (in dbSNP:rs2306031).
/FTId=VAR_058292.
VARIANT 1277 1277 R -> H (in CMS17; decreases binding
affinity for AGRN and MUSK proteins; does
not enhance downstream activation of the
MUSK signaling pathway thus impairing
clustering of AChRs; dbSNP:rs746136135).
{ECO:0000269|PubMed:24234652}.
/FTId=VAR_073696.
VARIANT 1554 1554 S -> G (in dbSNP:rs2306029).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9693030,
ECO:0000269|Ref.1}.
/FTId=VAR_057956.
VARIANT 1646 1646 R -> Q (in dbSNP:rs3816614).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9693030,
ECO:0000269|Ref.1}.
/FTId=VAR_057957.
MUTAGEN 1214 1214 N->A: Compromises Wnt-suppressive
activity. {ECO:0000269|PubMed:24234652}.
MUTAGEN 1252 1252 V->A: Compromises AGRN-mediated up-
regulation of MUSK signaling.
{ECO:0000269|PubMed:24234652}.
MUTAGEN 1256 1256 Y->A: Compromises Wnt-suppressive
activity. {ECO:0000269|PubMed:24234652}.
MUTAGEN 1287 1287 I->A: Compromises AGRN-mediated up-
regulation of MUSK signaling.
{ECO:0000269|PubMed:24234652}.
CONFLICT 1472 1475 EPRA -> D (in Ref. 2; BAE19679).
{ECO:0000305}.
CONFLICT 1478 1478 V -> A (in Ref. 2; BAE19679).
{ECO:0000305}.
CONFLICT 1862 1862 T -> M (in Ref. 1; BAD83615 and 2;
BAA32468). {ECO:0000305}.
SEQUENCE 1905 AA; 212045 MW; A39117C18279F9AA CRC64;
MRRQWGALLL GALLCAHGLA SSPECACGRS HFTCAVSALG ECTCIPAQWQ CDGDNDCGDH
SDEDGCILPT CSPLDFHCDN GKCIRRSWVC DGDNDCEDDS DEQDCPPREC EEDEFPCQNG
YCIRSLWHCD GDNDCGDNSD EQCDMRKCSD KEFRCSDGSC IAEHWYCDGD TDCKDGSDEE
NCPSAVPAPP CNLEEFQCAY GRCILDIYHC DGDDDCGDWS DESDCSSHQP CRSGEFMCDS
GLCINAGWRC DGDADCDDQS DERNCTTSMC TAEQFRCHSG RCVRLSWRCD GEDDCADNSD
EENCENTGSP QCALDQFLCW NGRCIGQRKL CNGVNDCGDN SDESPQQNCR PRTGEENCNV
NNGGCAQKCQ MVRGAVQCTC HTGYRLTEDG HTCQDVNECA EEGYCSQGCT NSEGAFQCWC
ETGYELRPDR RSCKALGPEP VLLFANRIDI RQVLPHRSEY TLLLNNLENA IALDFHHRRE
LVFWSDVTLD RILRANLNGS NVEEVVSTGL ESPGGLAVDW VHDKLYWTDS GTSRIEVANL
DGAHRKVLLW QNLEKPRAIA LHPMEGTIYW TDWGNTPRIE ASSMDGSGRR IIADTHLFWP
NGLTIDYAGR RMYWVDAKHH VIERANLDGS HRKAVISQGL PHPFAITVFE DSLYWTDWHT
KSINSANKFT GKNQEIIRNK LHFPMDIHTL HPQRQPAGKN RCGDNNGGCT HLCLPSGQNY
TCACPTGFRK ISSHACAQSL DKFLLFARRM DIRRISFDTE DLSDDVIPLA DVRSAVALDW
DSRDDHVYWT DVSTDTISRA KWDGTGQEVV VDTSLESPAG LAIDWVTNKL YWTDAGTDRI
EVANTDGSMR TVLIWENLDR PRDIVVEPMG GYMYWTDWGA SPKIERAGMD ASGRQVIISS
NLTWPNGLAI DYGSQRLYWA DAGMKTIEFA GLDGSKRKVL IGSQLPHPFG LTLYGERIYW
TDWQTKSIQS ADRLTGLDRE TLQENLENLM DIHVFHRRRP PVSTPCAMEN GGCSHLCLRS
PNPSGFSCTC PTGINLLSDG KTCSPGMNSF LIFARRIDIR MVSLDIPYFA DVVVPINITM
KNTIAIGVDP QEGKVYWSDS TLHRISRANL DGSQHEDIIT TGLQTTDGLA VDAIGRKVYW
TDTGTNRIEV GNLDGSMRKV LVWQNLDSPR AIVLYHEMGF MYWTDWGENA KLERSGMDGS
DRAVLINNNL GWPNGLTVDK ASSQLLWADA HTERIEAADL NGANRHTLVS PVQHPYGLTL
LDSYIYWTDW QTRSIHRADK GTGSNVILVR SNLPGLMDMQ AVDRAQPLGF NKCGSRNGGC
SHLCLPRPSG FSCACPTGIQ LKGDGKTCDP SPETYLLFSS RGSIRRISLD TSDHTDVHVP
VPELNNVISL DYDSVDGKVY YTDVFLDVIR RADLNGSNME TVIGRGLKTT DGLAVDWVAR
NLYWTDTGRN TIEASRLDGS CRKVLINNSL DEPRAIAVFP RKGYLFWTDW GHIAKIERAN
LDGSERKVLI NTDLGWPNGL TLDYDTRRIY WVDAHLDRIE SADLNGKLRQ VLVSHVSHPF
ALTQQDRWIY WTDWQTKSIQ RVDKYSGRNK ETVLANVEGL MDIIVVSPQR QTGTNACGVN
NGGCTHLCFA RASDFVCACP DEPDSRPCSL VPGLVPPAPR ATGMSEKSPV LPNTPPTTLY
SSTTRTRTSL EEVEGRCSER DARLGLCARS NDAVPAAPGE GLHISYAIGG LLSILLILVV
IAALMLYRHK KSKFTDPGMG NLTYSNPSYR TSTQEVKIEA IPKPAMYNQL CYKKEGGPDH
NYTKEKIKIV EGICLLSGDD AEWDDLKQLR SSRGGLLRDH VCMKTDTVSI QASSGSLDDT
ETEQLLQEEQ SECSSVHTAA TPERRGSLPD TGWKHERKLS SESQV


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